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TitleStructural and Theoretical Studies Indicate that the Cylindrical Protease ClpP Samples Extended and Compact Conformations.
Journal, issue, pagesStructure, Vol. 18, Page 798-808, Year 2010
Publish dateMay 27, 2009 (structure data deposition date)
AuthorsKimber, M.S. / Yu, A.Y. / Borg, M. / Leung, E. / Chan, H.S. / Houry, W.A.
External linksStructure / PubMed:20637416
MethodsX-ray diffraction
Resolution3.2 Å
Structure data

PDB-3hln:
Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / disulfide bond / disordered equatorial loops / ATP-binding / Nucleotide-binding / Protease / Serine protease / Stress response / Zymogen

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