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Structure paper

TitleCrystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation.
Journal, issue, pagesEMBO J., Vol. 17, Page 5227-5237, Year 1998
Publish dateJan 27, 1999 (structure data deposition date)
AuthorsSchmitt, E. / Moulinier, L. / Fujiwara, S. / Imanaka, T. / Thierry, J.C. / Moras, D.
External linksEMBO J. / PubMed:9724658
MethodsX-ray diffraction
Resolution1.89 - 2.4 Å
Structure data

PDB-1b8a:
ASPARTYL-TRNA SYNTHETASE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3nel:
Aspartyl-tRNA synthetase complexed with aspartic acid
Method: X-RAY DIFFRACTION / Resolution: 1.954 Å

PDB-3nem:
Aspartyl-tRNA synthetase complexed with aspartyl adenylate
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-3nen:
Unliganded aspartyl-tRNA synthetase from thermococcus kodakarensis
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-MN:
Unknown entry

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

ChemComp-HOH:
WATER

ChemComp-ASP:
ASPARTIC ACID

ChemComp-AMO:
ASPARTYL-ADENOSINE-5'-MONOPHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • thermococcus kodakarensis (archaea)
KeywordsLIGASE / SYNTHETASE / TRNA LIGASE / aminoacyl-tRNA synthetase / Rossmann fold OB fold / amino acid / Mg / tRNA / Rossmann Fold / OB Fold / Aspartic acid / ATP-Mg

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