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TitleReversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX Association.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 54, Page 15892-15896, Year 2015
Publish dateSep 4, 2015 (structure data deposition date)
AuthorsPahl, A. / Lakemeyer, M. / Vielberg, M.T. / Hackl, M.W. / Vomacka, J. / Korotkov, V.S. / Stein, M.L. / Fetzer, C. / Lorenz-Baath, K. / Richter, K. ...Pahl, A. / Lakemeyer, M. / Vielberg, M.T. / Hackl, M.W. / Vomacka, J. / Korotkov, V.S. / Stein, M.L. / Fetzer, C. / Lorenz-Baath, K. / Richter, K. / Waldmann, H. / Groll, M. / Sieber, S.A.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:26566002
MethodsX-ray diffraction
Resolution3 Å
Structure data

PDB-5dl1:
ClpP from Staphylococcus aureus in complex with AV145
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-5C2:
1-(propan-2-yl)-N-{[2-(thiophen-2-yl)-1,3-oxazol-4-yl]methyl}-1H-pyrazolo[3,4-b]pyridine-5-carboxamide

Source
  • staphylococcus aureus (bacteria)
KeywordsHYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex / caseinolytic protease / allosteric regulation / binding analysis

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