DB code: S00523

CATH domain 3.30.1060.10 : Peptide Methionine Sulfoxide Reductase; Chain A Catalytic domain
E.C. 1.8.4.11
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.30.1060.10 : Peptide Methionine Sulfoxide Reductase; Chain A S00277

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0A5L0 Peptide methionine sulfoxide reductase msrA
Protein-methionine-S-oxide reductase
EC 1.8.4.11
Peptide-methionine (S)-S-oxide reductase
Peptide Met(O) reductase
NP_214651.1 (Protein)
NC_000962.3 (DNA/RNA sequence)
NP_334555.1 (Protein)
NC_002755.2 (DNA/RNA sequence)
YP_006513456.1 (Protein)
NC_018143.1 (DNA/RNA sequence)
PF01625 (PMSR)
[Graphical View]

KEGG enzyme name
peptide-methionine (S)-S-oxide reductase
MsrA
methionine sulfoxide reductase (ambiguous)
methionine sulphoxide reductase A
methionine S-oxide reductase (ambiguous)
methionine S-oxide reductase (S-form oxidizing)
methionine sulfoxide reductase A
peptide methionine sulfoxide reductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A5L0 MSRA_MYCTU Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C03895 C00342 C15999 C03023 C00343 C00001 C00073
E.C.
Compound Peptide-L-methionine (S)-S-oxide Reduced thioredoxin L-methionine (S)-S-oxide Peptide-L-methionine Oxidized thioredoxin H2O L-methionine
Type peptide/protein,sulfoxide group amide group,carbohydrate,peptide/protein,sulfhydryl group amino acids,sulfoxide group peptide/protein,sulfide group amide group,carbohydrate,disulfide bond,peptide/protein H2O amino acids,sulfide group
ChEBI 49031
 58772
 49031
 58772
 		15377
 15377
 		16643
 57844
 16643
 57844
PubChem 10909908
 11869257
 10909908
 11869257
 		22247451
 962
 22247451
 962
 		6137
 6992087
 6137
 6992087
1nwaA Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1fvg

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1nwaA CYS 13;TYR 44;GLU 52;TYR 92;CYS 154

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.3, p.13310-13311
[2]
Fig.1, p.35911-35913
[4]
Fig.3, p.6466-6467
[5]
Fig.8, p.1175-1176
[9]
Scheme 5, p.402-404
[15]
p.4121-4125

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)
Medline ID 20519025
PubMed ID 11063566
Journal Biochemistry
Year 2000
Volume 39
Pages 13307-12
Authors Lowther WT, Brot N, Weissbach H, Matthews BW
Title Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme.
Related PDB 1fva 1fvg
Related UniProtKB P54149
[2]
Resource
Comments
Medline ID
PubMed ID 10964927
Journal J Biol Chem
Year 2000
Volume 275
Pages 35908-13
Authors Boschi-Muller S, Azza S, Sanglier-Cianferani S, Talfournier F, Van Dorsselear A, Branlant G
Title A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10799493
Journal J Biol Chem
Year 2000
Volume 275
Pages 14167-72
Authors Moskovitz J, Poston JM, Berlett BS, Nosworthy NJ, Szczepanowski R, Stadtman ER
Title Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10841552
Journal Proc Natl Acad Sci U S A
Year 2000
Volume 97
Pages 6463-8
Authors Lowther WT, Brot N, Weissbach H, Honek JF, Matthews BW
Title Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11080639
Journal Structure Fold Des
Year 2000
Volume 8
Pages 1167-78
Authors Tete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, Aubry A
Title Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution.
Related PDB 1ff3
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11311146
Journal Biochem J
Year 2001
Volume 355
Pages 819-25
Authors Petropoulos I, Mary J, Perichon M, Friguet B
Title Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11430764
Journal J Biomol NMR
Year 2001
Volume 20
Pages 97-8
Authors Beraud S, Chambost JP, Bersch B, Gans P, Barras F, Marion D
Title Backbone H(N), N, Calpha, C' and Cbeta assignment of the 25 kDa peptide methionine sulfoxide reductase from Erwinia chrysanthemi.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11604533
Journal Protein Sci
Year 2001
Volume 10
Pages 2272-9
Authors Boschi-Muller S, Azza S, Branlant G
Title E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11860363
Journal Curr Med Chem
Year 2002
Volume 9
Pages 385-409
Authors Vaughan MD, Sampson PB, Honek JF
Title Methionine in and out of proteins: targets for drug design.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12431100
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 13709-15
Authors Beraud S, Bersch B, Brutscher B, Gans P, Barras F, Blackledge M
Title Direct structure determination using residual dipolar couplings: reaction-site conformation of methionine sulfoxide reductase in solution.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11812798
Journal J Biol Chem
Year 2002
Volume 277
Pages 12016-22
Authors Olry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, Van Dorsselear A, Branlant G
Title Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11885278
Journal Methods Enzymol
Year 2002
Volume 348
Pages 249-59
Authors Davis DA, Newcomb FM, Moskovitz J, Fales HM, Levine RL, Yarchoan R
Title Reversible oxidation of HIV-2 protease.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11938352
Journal Nat Struct Biol
Year 2002
Volume 9
Pages 348-52
Authors Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW
Title The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11807942
Journal Proteins
Year 2002
Volume 46
Pages 149-52
Authors Gladyshev VN
Title Thioredoxin and peptide methionine sulfoxide reductase: convergence of similar structure and function in distinct structural folds.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 12837786
Journal J Bacteriol
Year 2003
Volume 185
Pages 4119-26
Authors Taylor AB, Benglis DM Jr, Dhandayuthapani S, Hart PJ
Title Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.
Related PDB 1nwa
Related UniProtKB

Comments
The E.C. was transferred from 1.8.4.6 to 1.8.4.11.
This enzyme catalyzes two successive raections (see [1], [2], [4], [5], [9] & [15]):
(A) Reduction of L-methionine S-oxide.
(B) Reduction of active-site residues through oxidation of reduced thioredoxin.

Created Updated
2004-02-02 2009-02-26