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Structure paper

TitleATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
Journal, issue, pagesEMBO J., Vol. 22, Page 676-688, Year 2003
Publish dateNov 12, 2002 (structure data deposition date)
AuthorsSekine, S. / Nureki, O. / Dubois, D.Y. / Bernier, S. / Chenevert, R. / Lapointe, J. / Vassylyev, D.G. / Yokoyama, S.
External linksEMBO J. / PubMed:12554668
MethodsX-ray diffraction
Resolution1.8 - 2.4 Å
Structure data

PDB-1j09:
Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP and Glu
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1n75:
Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP.
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1n77:
Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(Glu) and ATP.
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1n78:
Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(Glu) and glutamol-AMP.
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-GOM:
GLUTAMOL-AMP

Source
  • thermus thermophilus (bacteria)
KeywordsLIGASE / GluRS-ATP-Glu complex / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics / ERS/ATP / Glutamyl-tRNA synthetase / ligase/RNA / ERS/tRNA/ATP / ligase-RNA COMPLEX / ERS/tRNA/GOA

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