Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli | |
Zn2+ | the presence of dynamically rigid zinc ion coordination sphere and bipartite mode of recognition of ectRNAThr are observed | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine + tRNAThr | Escherichia coli | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A8M3 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr | reaction mechanism and structure-function relationship, overview. Molecular dynamics simulation study of the dynamics of the active site organization during charging step of dimeric ThrRS from Escherichia coli (ecThrRS) bound with ectRNAThr | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine + tRNAThr | - |
Escherichia coli | AMP + diphosphate + L-threonyl-tRNAThr | - |
? | |
ATP + L-threonine + tRNAThr | Escherichia coli ectRNAThr | Escherichia coli | AMP + diphosphate + L-threonyl-tRNAThr | - |
? | |
additional information | the interaction of ecRNAThr with the enzyme, interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the dimeric ecThrRS composed of two noncovalently bound monomers bound with ectRNAThr. The anticodon arm of the bound tRNA recognizes the C-terminal anticodon binding domain and acceptor arm interacts with both N-terminal domain and catalytic domain of monomer | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ectRNAThr | - |
Escherichia coli |
threonyl tRNA synthetase | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the class II of aminoacyl-tRNA sythetases | Escherichia coli |
additional information | molecular dynamics simulation study of the dynamics of the active site organization during charging step of dimeric ThrRS from Escherichia coli (ecThrRS) bound with ectRNAThr. The active site residues of the motif 2 loop approach the proximal bases of tRNA and adenylate by slow diffusive motion (in nanosecond time scale) and make conformational changes of the respective side chains via ultrafast librational motion to develop precise hydrogen bond geometry. Presence of bound Mg2+ ions around tRNA and dynamically slow bound water are other common features of the enzyme. The presence of dynamically rigid zinc ion coordination sphere and bipartite mode of recognition of ectRNAThr are observed. Molecular dynamic simulation, overview | Escherichia coli |