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Structure paper

TitleConformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase
Journal, issue, pagesJ. Mol. Biol., Vol. 331, Page 201-211, Year 2003
Publish dateFeb 13, 2003 (structure data deposition date)
AuthorsTorres-Larios, A. / Sankaranarayanan, R. / Rees, B. / Dock-Bregeon, A.C. / Moras, D.
External linksJ. Mol. Biol. / PubMed:12875846
MethodsX-ray diffraction
Resolution2.8 - 3.2 Å
Structure data

PDB-1nyq:
Structure of Staphylococcus aureus threonyl-tRNA synthetase complexed with an analogue of threonyl adenylate
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-1nyr:
Structure of Staphylococcus aureus threonyl-tRNA synthetase complexed with ATP
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-TSB:
5'-O-(N-(L-THREONYL)-SULFAMOYL)ADENOSINE

ChemComp-HOH:
WATER

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

ChemComp-THR:
THREONINE

Source
  • staphylococcus aureus (bacteria)
KeywordsLIGASE / threonyl-tRNA synthetase / adenylate / ATP / threonine

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