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TitleIndependent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
Journal, issue, pagesProc. Natl. Acad. Sci. Usa, Vol. 106, Page 1790-1795, Year 2009
Publish dateDec 9, 2008 (structure data deposition date)
AuthorsLaowanapiban, P. / Kapustina, M. / Vonrhein, C. / Delarue, M. / Koehl, P. / Carter, C.W.
External linksProc. Natl. Acad. Sci. Usa / PubMed:19174517
MethodsX-ray diffraction
Resolution2.65 - 2.7 Å
Structure data

PDB-3fhj:
Independent saturation of three TrpRS subsites generates a partially-assembled state similar to those observed in molecular simulations
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-3fi0:
Crystal Structure Analysis of B. stearothermophilus Tryptophanyl-tRNA Synthetase Complexed with Tryptophan, AMP, and Inorganic Phosphate
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-TRP:
TRYPTOPHAN

ChemComp-PO4:
PHOSPHATE ION

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • bacillus stearothermophilus (bacteria)
KeywordsTRANSLATION / ligand-dependent domain rearrangement / mechanistic pathway / molecular simulations / Aminoacyl-tRNA synthetase / ATP-binding / Cytoplasm / Ligase / Nucleotide-binding / Protein biosynthesis / Domain rearrangement

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