Protein Variants | Comment | Organism |
---|---|---|
E222K | site-directed mutagenesis, mutational structure-function study, the residue is part of the invariant Hub, the mutation leads to mischarging and affected cognate tRNAGln recognition | Escherichia coli |
F90L | site-directed mutagenesis, mutational structure-function study, the residue is part of the connection in the active site network, the mutant shows increased Glu recognition in vitro and in vivo | Escherichia coli |
Q255I | site-directed mutagenesis, mutational structure-function study, the residue is part of the invariant Hub, the mutation leads to reduced specificity for cognate Gln recognition and increased Glu recognition | Escherichia coli |
R341A | site-directed mutagenesis, mutational structure-function study, the residue is part of the Hub common to all liganded complex, the mutation affects anticodon recognition | Escherichia coli |
Y211H | site-directed mutagenesis, mutational structure-function study, the residue is part of the connection in the quaternary cognate-complex, the mutants shows slow solvation dynamics in the active site | Escherichia coli |
Y240E/G | site-directed mutagenesis, mutational structure-function study, the residue is part of the Hub common to ligand-free and quaternary cognate-complex, the mutant shows increased Glu recognition in vitro and in vivo | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + tRNAGln | Escherichia coli | - |
AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P00962 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + tRNAGln | - |
Escherichia coli | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? | |
additional information | ternary complexed GlnRS bound to tRNAGln and the Gln-AMP analogue is catalytically active and has undergone the first step of the aminoacylation reaction | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | GlnRS structure networks, detection method development for accounting side chain interactions, yet providing a global view of the ligand-induced conformational changes, and understand allosteric changes mediated by the binding of ligands, usage of crystal structures: PDB IDs 1nyl, 1qtq, 1o0b, and 1o0c, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
Glutaminyl-tRNA synthetase | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |