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Literature summary for 6.1.1.3 extracted from

  • Wei, W.; Gauld, J.; Monard, G.
    Pretransfer editing in threonyl-tRNA synthetase roles of differential solvent accessibility and intermediate stabilization (2017), ACS Catal., 7, 3102-3112 .
No PubMed abstract available
Search for more literature for 6.1.1.3

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-threonine + tRNAThr Saccharomyces cerevisiae
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr reaction mechanism and structure-function relationship, modeling, overview Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-threonine + tRNAThr
-
 Saccharomyces cerevisiae AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
additional information residues Gln180 and Gln292 are important in cofactor binding Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
Mst1
-
 Saccharomyces cerevisiae
Threonyl-tRNA synthetase
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information analysis of pre-transfer editing mechanism in yeast mitochondrial threonyl-tRNA synthetase (MST1) via the combined application of classical molecular dynamics and QM/MM-MD free energy calculations. The X-ray crystal structure of a single monomer of MST1 from Saccharomyces cerevisiae, PDB ID 3UH0 at 2.0 A resolution, is used as the starting structure for the computational studies. Molecular dynamics simulations, overview. Residues Gln180 and Gln292 are important in cofactor binding, Gln180 and Gln292 do not alternate in their H bonding to the Ser-AMP phosphate. Water molecules are able to enter and replace the H bonding networks and, as a result, MST1-bound Ser-AMP has increased variability in its positioning within the active site in comparison to Thr-AMP. A H-bond is intermittently formed between the alpha-amino group of the Thr and Ser and the side chain hydroxyl of Tyr270, though with markedly greater occurrence for Thr-AMP (22%) in comparison to Ser-AMP (7%). Mechanism of Thr-AMP and Ser-AMP hydrolysis determination by umbrella sampling on both ligands from three different initial conformations Saccharomyces cerevisiae
physiological function aminoacyl-tRNA synthetases (aaRSs) catalyze the activation of the corresponding amino acids and attachment to their cognate tRNAs with extremely high fidelity due to pre- and post-transfer editing processes Saccharomyces cerevisiae