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Structure paper

TitleHelix unfolding/refolding characterizes the functional dynamics of Staphylococcus aureus Clp protease
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 17643-17653, Year 2013
Publish dateApr 12, 2012 (structure data deposition date)
AuthorsYe, F. / Zhang, J. / Liu, H. / Hilgenfeld, R. / Zhang, R. / Kong, X. / Li, L. / Lu, J. / Zhang, X. / Li, D. ...Ye, F. / Zhang, J. / Liu, H. / Hilgenfeld, R. / Zhang, R. / Kong, X. / Li, L. / Lu, J. / Zhang, X. / Li, D. / Jiang, H. / Yang, C.-G. / Luo, C.
External linksJ. Biol. Chem. / PubMed:23625918
MethodsX-ray diffraction
Resolution2.4 - 2.7 Å
Structure data

PDB-4emm:
Crystal structure of Staphylococcus aureus ClpP in compact conformation
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-4emp:
Crystal structure of the mutant of ClpP E137A from Staphylococcus aureus
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • staphylococcus aureus (bacteria)
KeywordsHYDROLASE / tetradecameric chamber / protein binding / ATP-dependent Clp protease proteolytic subunit

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