DB code: M00049
| RLCP classification | 3.113.90000.394 : Transfer | |
|---|---|---|
| CATH domain | 3.10.20.30 : Ubiquitin-like (UB roll) | |
| 3.30.980.10 : Threonyl-tRNA Synthetase; Chain A, domain 2 | ||
| 3.30.54.20 : Replication Terminator Protein; Chain A, domain 2 | ||
| 3.30.930.10 : BirA Bifunctional Protein; domain 2 | Catalytic domain | |
| 3.40.50.800 : Rossmann fold | ||
| E.C. | 6.1.1.3 | |
| CSA | 1qf6 | |
| M-CSA | 1qf6 | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.10.20.30 : Ubiquitin-like (UB roll) | M00039 M00042 |
| 3.30.930.10 : BirA Bifunctional Protein; domain 2 | S00413 D00291 D00293 D00294 D00295 T00113 |
| 3.40.50.800 : Rossmann fold | D00295 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0A8M3 |
Threonyl-tRNA synthetase
|
EC
6.1.1.3
Threonine--tRNA ligase ThrRS |
NP_416234.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_489981.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF03129
(HGTP_anticodon)
PF02824 (TGS) PF00587 (tRNA-synt_2b) PF07973 (tRNA_SAD) [Graphical View] |
| Q8NW68 |
Threonyl-tRNA synthetase
|
EC
6.1.1.3
Threonine--tRNA ligase ThrRS |
NP_646443.1
(Protein)
NC_003923.1 (DNA/RNA sequence) |
PF03129
(HGTP_anticodon)
PF02824 (TGS) PF00587 (tRNA-synt_2b) PF07973 (tRNA_SAD) [Graphical View] |
| KEGG enzyme name |
|---|
|
threonine---tRNA ligase
threonyl-tRNA synthetase threonyl-transfer ribonucleate synthetase threonyl-transfer RNA synthetase threonyl-transfer ribonucleic acid synthetase threonyl ribonucleic synthetase threonine-transfer ribonucleate synthetase threonine translase threonyl-tRNA synthetase TRS |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0A8M3 | SYT_ECOLI | ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). | Homodimer. | Cytoplasm. | Binds 1 zinc ion per subunit. |
| Q8NW68 | SYT_STAAW | ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). | Homodimer (By similarity). | Cytoplasm. | Binds 1 zinc ion per subunit (By similarity). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00260 | Glycine, serine and threonine metabolism | |
| MAP00970 | Aminoacyl-tRNA biosynthesis |
| Compound table | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00038 | C00305 | C00002 | C00188 | C01651 | C00013 | C00020 | C02992 | ||||||
| E.C. | ||||||||||||||
| Compound | Zinc | Magnesium | ATP | L-Threonine | tRNA(Thr) | Pyrophosphate | AMP | L-Threonyl-tRNA(Thr) | ||||||
| Type | heavy metal | divalent metal (Ca2+, Mg2+) | amine group,nucleotide | amino acids,carbohydrate | nucleic acids | phosphate group/phosphate ion | amine group,nucleotide | amino acids,carbohydrate,nucleic acids | ||||||
| ChEBI |
29105 29105 |
18420 18420 |
15422 15422 |
16857 57926 16857 57926 |
29888 29888 |
16027 16027 |
||||||||
| PubChem |
32051 32051 |
888 888 |
5957 5957 |
6288 6971019 6288 6971019 |
1023 21961011 1023 21961011 |
6083 6083 |
||||||||
| 1qf6A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1qf6A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqB02 |
|
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrB02 |
|
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1qf6A03 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqA03 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqB03 |
|
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrA03 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrB03 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evkA01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evkB01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Bound:THR | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evlA01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1evlB01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1evlC01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1evlD01 |
|
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1fyfA01 |
|
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:SSA |
| 1fyfB01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:SSA |
| 1kogA01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1kogB01 |
|
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1kogC01 |
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1kogD01 |
|
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1kogE01 |
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1kogF01 |
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1kogG01 |
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1kogH01 |
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1qf6A04 |
|
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|
|
Bound:_ZN | Unbound | Unbound | Unbound | Bound:__A_76(chain B) | Unbound | Bound:AMP | Unbound | Unbound |
| 1nyqA04 |
|
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|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1nyqB04 |
|
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Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:TSB |
| 1nyrA04 |
|
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Bound:_ZN | Unbound | Bound:ATP | Bound:THR | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrB04 |
|
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Bound:_ZN | Unbound | Bound:ATP | Bound:THR | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evkA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evkB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evlA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evlB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evlC02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1evlD02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1fyfA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1fyfB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogC02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogD02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogE02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogF02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogG02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kogH02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1qf6A05 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqA05 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyqB05 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrA05 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1nyrB05 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P0A8M3 & literature [3] & [13] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1qf6A01 |
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| 1nyqA01 |
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| 1nyqB01 |
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| 1nyrA01 |
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| 1nyrB01 |
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| 1qf6A02 |
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| 1nyqA02 |
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| 1nyqB02 |
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| 1nyrA02 |
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| 1nyrB02 |
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| 1qf6A03 |
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| 1nyqA03 |
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| 1nyqB03 |
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| 1nyrA03 |
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| 1nyrB03 |
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| 1evkA01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1evkB01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1evlA01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1evlB01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1evlC01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1evlD01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1fyfA01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1fyfB01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogA01 |
|
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|
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogB01 |
|
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|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogC01 |
|
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|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogD01 |
|
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|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogE01 |
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogF01 |
|
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|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogG01 |
|
|
|
|
|
ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1kogH01 |
|
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|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1qf6A04 |
|
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|
|
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ARG 363;ARG 375;LYS 465 | CYS 334;HIS 385;HIS 511(Zinc binding);GLU 365(Magnesium binding) | |||
| 1nyqA04 |
|
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ARG 365;ARG 377;LYS 471 | CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding) | |||
| 1nyqB04 |
|
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ARG 365;ARG 377;LYS 471 | CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding) | |||
| 1nyrA04 |
|
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ARG 365;ARG 377;LYS 471 | CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding) | |||
| 1nyrB04 |
|
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ARG 365;ARG 377;LYS 471 | CYS 336;HIS 387;HIS 517(Zinc binding);GLU 367(Magnesium binding) | |||
| 1evkA02 |
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| 1evkB02 |
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| 1evlA02 |
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| 1evlB02 |
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| 1evlC02 |
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| 1evlD02 |
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| 1fyfA02 |
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| 1fyfB02 |
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| 1kogA02 |
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| 1kogB02 |
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| 1kogC02 |
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| 1kogD02 |
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| 1kogE02 |
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| 1kogF02 |
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| 1kogG02 |
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| 1kogH02 |
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| 1qf6A05 |
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| 1nyqA05 |
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| 1nyqB05 |
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| 1nyrA05 |
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| 1nyrB05 |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[7]
|
Fig.1, p.435 | |
|
[13]
|
p.206-207 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2388270 |
| Journal | J Mol Biol |
| Year | 1990 |
| Volume | 214 |
| Pages | 819-20 |
| Authors | Garber MB, Yaremchuk AD, Tukalo MA, Egorova SP, Fomenkova NP, Nikonov SV |
| Title |
Crystals of threonyl-tRNA synthetase from Thermus thermophilus. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7589494 |
| Journal | FEBS Lett |
| Year | 1995 |
| Volume | 374 |
| Pages | 110-2 |
| Authors | Cura V, Kern D, Mitschler A, Moras D |
| Title | Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). |
| Medline ID | 99251535 |
| PubMed ID | 10319817 |
| Journal | Cell |
| Year | 1999 |
| Volume | 97 |
| Pages | 371-81 |
| Authors | Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D |
| Title | The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. |
| Related PDB | 1qf6 |
| Related UniProtKB | P0A8M3 |
| [4] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 11136973 |
| Journal | Cell |
| Year | 2000 |
| Volume | 103 |
| Pages | 877-84 |
| Authors | Dock-Bregeon A, Sankaranarayanan R, Romby P, Caillet J, Springer M, Rees B, Francklyn CS, Ehresmann C, Moras D |
| Title |
Transfer RNA-mediated editing in threonyl-tRNA synthetase. |
| Related PDB | 1fyf |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10675344 |
| Journal | EMBO J |
| Year | 2000 |
| Volume | 19 |
| Pages | 749-57 |
| Authors | Staker BL, Korber P, Bardwell JC, Saper MA |
| Title | Structure of Hsp15 reveals a novel RNA-binding motif. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10632708 |
| Journal | Eur J Biochem |
| Year | 2000 |
| Volume | 267 |
| Pages | 379-93 |
| Authors | Cura V, Moras D, Kern D |
| Title | Sequence analysis and modular organization of threonyl-tRNA synthetase from Thermus thermophilus and its interrelation with threonyl-tRNA synthetases of other origins. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10881182 |
| Journal | Nat Struct Biol |
| Year | 2000 |
| Volume | 7 |
| Pages | 435-6 |
| Authors | Musier-Forsyth K, Beuning PJ |
| Title | Role of zinc ion in translational accuracy becomes crystal clear. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 242-642. |
| Medline ID | 20343005 |
| PubMed ID | 10881191 |
| Journal | Nat Struct Biol |
| Year | 2000 |
| Volume | 7 |
| Pages | 461-5 |
| Authors | Sankaranarayanan R, Dock-Bregeon AC, Rees B, Bovee M, Caillet J, Romby P, Francklyn CS, Moras D |
| Title | Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase. |
| Related PDB | 1evk 1evl |
| Related UniProtKB | P0A8M3 |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11732604 |
| Journal | Acta Biochim Pol |
| Year | 2001 |
| Volume | 48 |
| Pages | 323-35 |
| Authors | Sankaranarayanan R, Moras D |
| Title | The fidelity of the translation of the genetic code. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11953757 |
| Journal | Nat Struct Biol |
| Year | 2002 |
| Volume | 9 |
| Pages | 343-7 |
| Authors | Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D |
| Title | Structural basis of translational control by Escherichia coli threonyl tRNA synthetase. |
| Related PDB | 1kog |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14690420 |
| Journal | Biochemistry |
| Year | 2003 |
| Volume | 42 |
| Pages | 15102-13 |
| Authors | Bovee ML, Pierce MA, Francklyn CS |
| Title | Induced fit and kinetic mechanism of adenylation catalyzed by Escherichia coli threonyl-tRNA synthetase. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12554667 |
| Journal | EMBO J |
| Year | 2003 |
| Volume | 22 |
| Pages | 668-75 |
| Authors | Beebe K, Ribas De Pouplana L, Schimmel P |
| Title | Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12875846 |
| Journal | J Mol Biol |
| Year | 2003 |
| Volume | 331 |
| Pages | 201-11 |
| Authors | Torres-Larios A, Sankaranarayanan R, Rees B, Dock-Bregeon AC, Moras D |
| Title |
Conformational movements and cooperativity upon amino acid, |
| Related PDB | 1nyr |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12581352 |
| Journal | Mol Microbiol |
| Year | 2003 |
| Volume | 47 |
| Pages | 961-74 |
| Authors | Caillet J, Nogueira T, Masquida B, Winter F, Graffe M, Dock-Bregeon AC, Torres-Larios A, Sankaranarayanan R, Westhof E, Ehresmann B, Ehresmann C, Romby P, Springer M |
| Title | The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the class-IIa aminoacyl-tRNA synthetase family.
Although the tertiary structures with magnesium ions have not been determined yet, According to the literature [7] & [8], According to the literature [13], The first transfer reaction proceeds as follows (see [13]): (1) The first substrate, (2) Arg363 stabilizes the negatively charged groups, (3) The stabilization of the negatively charged groups leads to an in-line nucleophilic attack by the carboxylate group on the alpha-phosphorus atom, (4) The pentacovalent transition state is stabilized by three basic residues (Arg363, (5) The leaving group, The second acyl transfer reaction has not been elucidated yet. |
| Created | Updated |
|---|---|
| 2004-10-25 | 2009-04-03 |