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TitleMechanism of elongation factor-G-mediated fusidic acid resistance and fitness compensation in Staphylococcus aureus.
Journal, issue, pagesJ. Biol. Chem., Vol. 287, Page 30257-30267, Year 2012
Publish dateAug 30, 2011 (structure data deposition date)
AuthorsKoripella, R.K. / Chen, Y. / Peisker, K. / Koh, C.S. / Selmer, M. / Sanyal, S.
External linksJ. Biol. Chem. / PubMed:22767604
MethodsX-ray diffraction
Resolution2.8 - 2.98 Å
Structure data

PDB-3zz0:
Crystal structure of ribosomal elongation factor (EF)-G from Staphylococcus aureus with a fusidic acid hyper-sensitivity mutation M16I
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3zzt:
Crystal structure of Staphylococcus aureus elongation factor G with a fusidic-acid-resistant mutation F88L
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-3zzu:
Crystal structure of Staphylococcus aureus elongation factor G with mutations M16I and F88L
Method: X-RAY DIFFRACTION / Resolution: 2.98 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • staphylococcus aureus (bacteria)
KeywordsTRANSLATION / GTPASE / FIVE-DOMAIN STRUCTURE

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