M00186
type: Enzyme
cath: TIM Barrel
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
cath: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
cath: Nucleotidyltransferase; domain 5
cath: DNA Polymerase III; Chain A
cath: Rossmann fold
cath: Zinc Finger, Delta Prime; domain 3
cath: Helicase, Ruva Protein; domain 3
cath: DNA Polymerase III; Chain A, domain 2
ec: https://purl.uniprot.org/enzyme/2.7.7.7
ec: https://purl.uniprot.org/enzyme/3.1.11.1
ec: https://purl.uniprot.org/enzyme/3.6.1.3
csa: 1j53
uniprot: P10443
uniprot: P03007
uniprot: P0ABS8
uniprot: P06710
uniprot: P28630
uniprot: P28631
uniprot: P28632
uniprot: P28905
uniprot: P0A988
kegg enzyme: DNA-directed DNA polymerase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.7
kegg pathway: Purine metabolism
kegg pathway: Pyrimidine metabolism
kegg cofactor: Divalent metal
kegg substrate: Deoxynucleoside triphosphate
kegg substrate: DNA(n)
kegg substrate: H2O
kegg substrate: ATP
kegg product: Pyrophosphate
kegg product: DNA(n)
kegg product: 5'-Phosphomononucleotides
kegg product: ADP
kegg product: Orthophosphate
pdb: 1j53A
pdb: 1j54A
pdb: 1du2A
pdb: 2ae9A
pdb: 1jr3A01
pdb: 1jr3B01
pdb: 1jr3C01
pdb: 1xxhB01
pdb: 1xxhC01
pdb: 1xxhD01
pdb: 1xxhG01
pdb: 1xxhH01
pdb: 1xxhI01
pdb: 1xxiB01
pdb: 1xxiC01
pdb: 1xxiD01
pdb: 1xxiG01
pdb: 1xxiH01
pdb: 1xxiI01
pdb: 1njfA01
pdb: 1njfB01
pdb: 1njfC01
pdb: 1njfD01
pdb: 1njgA01
pdb: 1njgB01
pdb: 1jr3A02
pdb: 1jr3B02
pdb: 1jr3C02
pdb: 1xxhB02
pdb: 1xxhC02
pdb: 1xxhD02
pdb: 1xxhG02
pdb: 1xxhH02
pdb: 1xxhI02
pdb: 1xxiB02
pdb: 1xxiC02
pdb: 1xxiD02
pdb: 1xxiG02
pdb: 1xxiH02
pdb: 1xxiI02

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.140
catalytic domain: index.html

OB fold (Dihydrolipoamide Acetyltransferase, E2P)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.50.140

Nucleotidyltransferase; domain 5
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.420.10
catalytic domain: index.html

DNA Polymerase III; Chain A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.1110.10

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.300
catalytic domain: index.html

Zinc Finger, Delta Prime; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.272.10

Helicase, Ruva Protein; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.8.60

Zinc Finger, Delta Prime; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.20.272.20

Helicase, Ruva Protein; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.8.10

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.10220

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.10110

DNA Polymerase III; Chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.10.150.10

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230
ec: https://purl.uniprot.org/enzyme/2.7.7.7
ec: https://purl.uniprot.org/enzyme/3.6.1.3

Pyrimidine metabolism
type: KeggPathway
references: KEGG:MAP00240
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Divalent metal
type: KeggCofactor
references: KEGG:C02148
ec: https://purl.uniprot.org/enzyme/2.7.7.7
ec: https://purl.uniprot.org/enzyme/3.1.11.1
compound type: divalent metal (Ca2+, Mg2+)

Deoxynucleoside triphosphate
type: KeggSubstrate
references: KEGG:C00677
ec: https://purl.uniprot.org/enzyme/2.7.7.7
compound type: nucleotide

DNA(n)
type: KeggSubstrate
references: KEGG:C00039
ec: https://purl.uniprot.org/enzyme/2.7.7.7
compound type: nucleic acids
label: DNA(n+1)
ec: https://purl.uniprot.org/enzyme/3.1.11.1
type: KeggProduct

H2O
type: KeggSubstrate
references: KEGG:C00001
ec: https://purl.uniprot.org/enzyme/3.1.11.1
ec: https://purl.uniprot.org/enzyme/3.6.1.3
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
references: KEGG:C00002
ec: https://purl.uniprot.org/enzyme/3.6.1.3
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyrophosphate
type: KeggProduct
references: KEGG:C00013
ec: https://purl.uniprot.org/enzyme/2.7.7.7
compound type: phosphate group/phosphate ion
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

5'-Phosphomononucleotides
type: KeggProduct
references: KEGG:C01150
ec: https://purl.uniprot.org/enzyme/3.1.11.1
compound type: nucleotide

ADP
type: KeggProduct
references: KEGG:C00008
ec: https://purl.uniprot.org/enzyme/3.6.1.3
compound type: amine group
compound type: nucleotide
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Orthophosphate
type: KeggProduct
references: KEGG:C00009
ec: https://purl.uniprot.org/enzyme/3.6.1.3
compound type: phosphate group/phosphate ion
references: CHEBI:26078
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1j53A
type: Pdb
references: 1j53
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j53
catalytic residue: GLU 14;HIS 162
cofactor binding residue: ASP 12;GLU 14;ASP 167(divalent metal binding)

1j54A
type: Pdb
references: 1j54
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j54
catalytic residue: GLU 14;HIS 162
cofactor binding residue: ASP 12;GLU 14;ASP 167(divalent metal binding)

1jr3A01
type: Pdb
references: 1jr3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jr3
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1jr3B01
type: Pdb
references: 1jr3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jr3
cofactor binding residue: CYS 2064;CYS 73;CYS 76;CYS 79(Zinc binding)

1jr3C01
type: Pdb
references: 1jr3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jr3
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxhB01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxhC01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxhD01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxhG01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxhH01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxhI01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxiB01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxiC01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxiD01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxiG01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxiH01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1xxiI01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1njfA01
type: Pdb
references: 1njf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1njf
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1njfB01
type: Pdb
references: 1njf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1njf
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1njfC01
type: Pdb
references: 1njf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1njf
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1njfD01
type: Pdb
references: 1njf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1njf
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1njgA01
type: Pdb
references: 1njg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1njg
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1njgB01
type: Pdb
references: 1njg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1njg
cofactor binding residue: CYS 64;CYS 73;CYS 76;CYS 79(Zinc binding)

1a5tA01
type: Pdb
references: 1a5t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5t
cofactor binding residue: CYS 50;CYS 59;CYS 62;CYS 65(Zinc binding)

1jr3E01
type: Pdb
references: 1jr3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jr3
cofactor binding residue: CYS 50;CYS 59;CYS 62;CYS 65(Zinc binding)

1xxhE01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 50;CYS 59;CYS 62;CYS 65(Zinc binding)

1xxhJ01
type: Pdb
references: 1xxh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxh
cofactor binding residue: CYS 50;CYS 59;CYS 62;CYS 65(Zinc binding)

1xxiE01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 50;CYS 59;CYS 62;CYS 65(Zinc binding)

1xxiJ01
type: Pdb
references: 1xxi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xxi
cofactor binding residue: CYS 50;CYS 59;CYS 62;CYS 65(Zinc binding)

Analogue
compound: ATP
pdb: 1xxhB01
ligand het code: ATG

Analogue
compound: ATP
pdb: 1xxhD01
ligand het code: ATG

Analogue
compound: ATP
pdb: 1xxhG01
ligand het code: ATG

Analogue
compound: ATP
pdb: 1xxhI01
ligand het code: ATG

Analogue
compound: ATP
pdb: 1njfA01
ligand het code: ATG

Analogue
compound: ATP
pdb: 1njfB01
ligand het code: ATG

Analogue
compound: ATP
pdb: 1njfD01
ligand het code: ATG

Analogue
compound: DNA(n)
pdb: 1j53A
ligand het code: TMP_2100

Analogue
compound: Orthophosphate
pdb: 1jr3A01
ligand het code: SO4

Analogue
compound: Orthophosphate
pdb: 1jr3B01
ligand het code: SO4

Analogue
compound: Orthophosphate
pdb: 1jr3C01
ligand het code: SO4

Analogue
compound: Orthophosphate
pdb: 1njgA01
ligand het code: SO4

Analogue
compound: Orthophosphate
pdb: 1njgB01
ligand het code: SO4

ReferenceForCatalyticMechanism
reference index: 34
reference section: Fig.5, p.540-543

The beta subunit of the DNA polymerase III holoenzyme becomes inaccessible to antibody after formation of an initiation complex with primed DNA.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7118945
journal: J Biol Chem
volume: 257
pages: 12310-5
published year: 1982
authors:
  item: Johanson KO
  item: McHenry CS

Proofreading by DNA polymerase III of Escherichia coli depends on cooperative interaction of the polymerase and exonuclease subunits.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3037519
journal: Proc Natl Acad Sci U S A
volume: 84
pages: 4389-92
published year: 1987
authors:
  item: Maki H
  item: Kornberg A

DNA Polymerase III holoenzyme of Escherichia coli. IV. The holoenzyme is an asymmetric dimer with twin active sites.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3283128
journal: J Biol Chem
volume: 263
pages: 6570-8
published year: 1988
authors:
  item: Maki H
  item: Maki S
  item: Kornberg A

Dissociation of the DNA polymerase III holoenzyme beta 2 subunits is accompanied by conformational change at distal cysteines 333.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2243096
journal: J Biol Chem
volume: 265
pages: 20356-63
published year: 1990
authors:
  item: Griep MA
  item: McHenry CS

DNA polymerase III holoenzyme. Components, structure, and mechanism of a true replicative complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1918028
journal: J Biol Chem
volume: 266
pages: 19127-30
published year: 1991
authors:
  item: McHenry CS

Accessory protein function in the DNA polymerase III holoenzyme from E. coli.
type: BibliographicResource
comment: REVIEW.
medline id: 92246902
references: http://www.ncbi.nlm.nih.gov/pubmed/1575709
journal: Bioessays
volume: 14
pages: 105-11
published year: 1992
authors:
  item: O'Donnell M
references: P28631

Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. II. Frequency of primer synthesis and efficiency of primer utilization control Okazaki fragment size.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1740452
journal: J Biol Chem
volume: 267
pages: 4045-53
published year: 1992
authors:
  item: Zechner EL
  item: Wu CA
  item: Marians KJ

Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
medline id: 92257585
references: http://www.ncbi.nlm.nih.gov/pubmed/1349852
journal: Cell
volume: 69
pages: 425-37
published year: 1992
authors:
  item: Kong XP
  item: Onrust R
  item: O'Donnell M
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00583

DNA polymerase III accessory proteins. II. Characterization of delta and delta'.
type: BibliographicResource
comment: CHARACTERIZATION.
medline id: 93280137
references: http://www.ncbi.nlm.nih.gov/pubmed/8505304
journal: J Biol Chem
volume: 268
pages: 11766-72
published year: 1993
authors:
  item: Onrust R
  item: O'Donnell M
references: P28631

Sliding clamps of DNA polymerases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7903401
journal: J Mol Biol
volume: 234
pages: 915-25
published year: 1993
authors:
  item: Kuriyan J
  item: O'Donnell M

DNA polymerase III accessory proteins. IV. Characterization of chi and psi.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8505305
journal: J Biol Chem
volume: 268
pages: 11779-84
published year: 1993
authors:
  item: Xiao H
  item: Dong Z
  item: O'Donnell M

Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8001157
journal: Cell
volume: 79
pages: 1233-43
published year: 1994
authors:
  item: Krishna TS
  item: Kong XP
  item: Gary S
  item: Burgers PM
  item: Kuriyan J

holE, the gene coding for the theta subunit of DNA polymerase III of Escherichia coli: characterization of a holE mutant and comparison with a dnaQ (epsilon-subunit) mutant.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8300534
journal: J Bacteriol
volume: 176
pages: 815-21
published year: 1994
authors:
  item: Slater SC
  item: Lifsics MR
  item: O'Donnell M
  item: Maurer R

Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7768937
journal: J Biol Chem
volume: 270
pages: 13358-65
published year: 1995
authors:
  item: Naktinis V
  item: Onrust R
  item: Fang L
  item: O'Donnell M

Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16199579
journal: J Bacteriol
volume: 187
pages: 7081-9
published year: 2005
authors:
  item: Mueller GA
  item: Kirby TW
  item: DeRose EF
  item: Li D
  item: Schaaper RM
  item: London RE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. III. Interface between two polymerases and the clamp loader.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7768938
journal: J Biol Chem
volume: 270
pages: 13366-77
published year: 1995
authors:
  item: Onrust R
  item: Finkelstein J
  item: Turner J
  item: Naktinis V
  item: O'Donnell M

Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. IV. ATP-binding site mutants identify the clamp loader.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7768939
journal: J Biol Chem
volume: 270
pages: 13378-83
published year: 1995
authors:
  item: Xiao H
  item: Naktinis V
  item: O'Donnell M

Structural and functional similarities of prokaryotic and eukaryotic DNA polymerase sliding clamps.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7478986
journal: Nucleic Acids Res
volume: 23
pages: 3613-20
published year: 1995
authors:
  item: Kelman Z
  item: O'Donnell M

Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 98028572
references: http://www.ncbi.nlm.nih.gov/pubmed/9363942
journal: Cell
volume: 91
pages: 335-45
published year: 1997
authors:
  item: Guenther B
  item: Onrust R
  item: Sali A
  item: O'Donnell M
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P28631

Fidelity of Escherichia coli DNA polymerase III holoenzyme. The effects of beta, gamma complex processivity proteins and epsilon proofreading exonuclease on nucleotide misincorporation efficiencies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9346941
journal: J Biol Chem
volume: 272
pages: 27919-30
published year: 1997
authors:
  item: Bloom LB
  item: Chen X
  item: Fygenson DK
  item: Turner J
  item: O'Donnell M
  item: Goodman MF

Translesional synthesis on DNA templates containing an estrogen quinone-derived adduct: N2-(2-hydroxyestron-6-yl)-2'-deoxyguanosine and N6-(2-hydroxyestron-6-yl)-2'-deoxyadenosine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9753470
journal: Biochemistry
volume: 37
pages: 13807-15
published year: 1998
authors:
  item: Terashima I
  item: Suzuki N
  item: Dasaradhi L
  item: Tan CK
  item: Downey KM
  item: Shibutani S

Phosphoesterase domains associated with DNA polymerases of diverse origins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9685491
journal: Nucleic Acids Res
volume: 26
pages: 3746-52
published year: 1998
authors:
  item: Aravind L
  item: Koonin EV

A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta' with DnaX(4) forms DnaX(3)deltadelta'.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11101526
journal: EMBO J
volume: 19
pages: 6536-45
published year: 2000
authors:
  item: Pritchard AE
  item: Dallmann HG
  item: Glover BP
  item: McHenry CS

NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10794414
journal: Protein Sci
volume: 9
pages: 721-33
published year: 2000
authors:
  item: Keniry MA
  item: Berthon HA
  item: Yang JY
  item: Miles CS
  item: Dixon NE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11525729
journal: Cell
volume: 106
pages: 429-41
published year: 2001
authors:
  item: Jeruzalmi D
  item: O'Donnell M
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Carboxyl-terminal domain III of the delta' subunit of the DNA polymerase III holoenzyme binds delta.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11518714
journal: J Biol Chem
volume: 276
pages: 40668-79
published year: 2001
authors:
  item: Song MS
  item: Dallmann HG
  item: McHenry CS

Carboxyl-terminal domain III of the delta' subunit of DNA polymerase III holoenzyme binds DnaX and supports cooperative DnaX complex assembly.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11606586
journal: J Biol Chem
volume: 276
pages: 48709-15
published year: 2001
authors:
  item: Song MS
  item: McHenry CS

Interplay of clamp loader subunits in opening the beta sliding clamp of Escherichia coli DNA polymerase III holoenzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11572866
journal: J Biol Chem
volume: 276
pages: 47185-94
published year: 2001
authors:
  item: Leu FP
  item: O'Donnell M

Mechanism of beta clamp opening by the delta subunit of Escherichia coli DNA polymerase III holoenzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11279099
journal: J Biol Chem
volume: 276
pages: 19182-9
published year: 2001
authors:
  item: Stewart J
  item: Hingorani MM
  item: Kelman Z
  item: O'Donnell M

Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11719243
journal: Curr Biol
volume: 11
pages: R935-46
published year: 2001
authors:
  item: O'Donnell M
  item: Jeruzalmi D
  item: Kuriyan J

Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11525728
journal: Cell
volume: 106
pages: 417-28
published year: 2001
authors:
  item: Jeruzalmi D
  item: Yurieva O
  item: Zhao Y
  item: Young M
  item: Stewart J
  item: Hingorani M
  item: O'Donnell M
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Analysis of a multicomponent thermostable DNA polymerase III replicase from an extreme thermophile.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11859073
journal: J Biol Chem
volume: 277
pages: 17334-48
published year: 2002
authors:
  item: Bruck I
  item: Yuzhakov A
  item: Yurieva O
  item: Jeruzalmi D
  item: Skangalis M
  item: Kuriyan J
  item: O'Donnell M

A three-domain structure for the delta subunit of the DNA polymerase III holoenzyme delta domain III binds delta' and assembles into the DnaX complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11809766
journal: J Biol Chem
volume: 277
pages: 13246-56
published year: 2002
authors:
  item: Bullard JM
  item: Pritchard AE
  item: Song MS
  item: Glover BP
  item: Wieczorek A
  item: Chen J
  item: Janjic N
  item: McHenry CS

Model for the catalytic domain of the proofreading epsilon subunit of Escherichia coli DNA polymerase III based on NMR structural data.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11772007
journal: Biochemistry
volume: 41
pages: 94-110
published year: 2002
authors:
  item: DeRose EF
  item: Li D
  item: Darden T
  item: Harvey S
  item: Perrino FW
  item: Schaaper RM
  item: London RE

Structural basis for proofreading during replication of the Escherichia coli chromosome.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11937058
journal: Structure
volume: 10
pages: 535-46
published year: 2002
authors:
  item: Hamdan S
  item: Carr PD
  item: Brown SE
  item: Ollis DL
  item: Dixon NE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14592985
journal: EMBO J
volume: 22
pages: 5883-92
published year: 2003
authors:
  item: Bunting KA
  item: Roe SM
  item: Pearl LH
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Flexibility revealed by the 1.85 A crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12832762
journal: Acta Crystallogr D Biol Crystallogr
volume: 59
pages: 1192-9
published year: 2003
authors:
  item: Oakley AJ
  item: Prosselkov P
  item: Wijffels G
  item: Beck JL
  item: Wilce MC
  item: Dixon NE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Nucleotide-induced conformational changes in an isolated Escherichia coli DNA polymerase III clamp loader subunit.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12623013
journal: Structure
volume: 11
pages: 253-63
published year: 2003
authors:
  item: Podobnik M
  item: Weitze TF
  item: O'Donnell M
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of the chi:psi sub-assembly of the Escherichia coli DNA polymerase clamp-loader complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14717711
journal: Eur J Biochem
volume: 271
pages: 439-49
published year: 2004
authors:
  item: Gulbis JM
  item: Kazmirski SL
  item: Finkelstein J
  item: Kelman Z
  item: O'Donnell M
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: II. Uncoupling the beta and DNA binding activities of the gamma complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14610068
journal: J Biol Chem
volume: 279
pages: 4386-93
published year: 2004
authors:
  item: Snyder AK
  item: Williams CR
  item: Johnson A
  item: O'Donnell M
  item: Bloom LB

Fluorescence measurements on the E.coli DNA polymerase clamp loader: implications for conformational changes during ATP and clamp binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15037068
journal: J Mol Biol
volume: 336
pages: 1047-59
published year: 2004
authors:
  item: Goedken ER
  item: Levitus M
  item: Johnson A
  item: Bustamante C
  item: O'Donnell M
  item: Kuriyan J

Structural and biochemical analysis of sliding clamp/ligand interactions suggest a competition between replicative and translesion DNA polymerases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14729336
journal: J Mol Biol
volume: 335
pages: 1187-97
published year: 2004
authors:
  item: Burnouf DY
  item: Olieric V
  item: Wagner J
  item: Fujii S
  item: Reinbolt J
  item: Fuchs RP
  item: Dumas P
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15556993
journal: Proc Natl Acad Sci U S A
volume: 101
pages: 16750-5
published year: 2004
authors:
  item: Kazmirski SL
  item: Podobnik M
  item: Weitze TF
  item: O'Donnell M
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

DNA polymerase I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase II
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase III
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase alpha
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase beta
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase gamma
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA nucleotidyltransferase (DNA-directed)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA nucleotidyltransferase (DNA-directed)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleate nucleotidyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxynucleate polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic acid duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic acid polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic polymerase I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA nucleotidyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA-dependent DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Klenow fragment
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

sequenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Taq DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Taq Pol I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Tca DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

exodeoxyribonuclease I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.11.1

Escherichia coli exonuclease I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.11.1

E. coli exonuclease I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.11.1

exonuclease I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.11.1

adenosinetriphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

adenylpyrophosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

ATP monophosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

triphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

ATPase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

SV40 T-antigen
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

adenosine 5'-triphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

ATP hydrolase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

ATPase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

complex V (mitochondrial electron transport)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

(Ca2+ + Mg2+)-ATPase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

HCO3--ATPase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3

adenosine triphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.3