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Structure paper

TitleFunctional Characterisation of ClpP Mutations Conferring Resistance to Acyldepsipeptide Antibiotics in Firmicutes.
Journal, issue, pagesChembiochem, Vol. 21, Page 1997-2012, Year 2020
Publish dateDec 30, 2019 (structure data deposition date)
AuthorsMalik, I.T. / Pereira, R. / Vielberg, M.T. / Mayer, C. / Straetener, J. / Thomy, D. / Famulla, K. / Castro, H. / Sass, P. / Groll, M. / Brotz-Oesterhelt, H.
External linksChembiochem / PubMed:32181548
MethodsX-ray diffraction
Resolution1.9 - 2.2 Å
Structure data

PDB-6tty:
Structure of ClpP from Staphylococcus aureus (apo, closed state)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6ttz:
Structure of the ClpP:ADEP4-complex from Staphylococcus aureus (open state)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NWT:
N-[(2S)-3-(3,5-difluorophenyl)-1-[[(3S,9S,13S,15R,19S,22S)-15,19-dimethyl-2,8,12,18,21-pentaoxo-11-oxa-1,7,17,20-tetrazatetracyclo[20.4.0.03,7.013,17]hexacosan-9-yl]amino]-1-oxopropan-2-yl]heptanamide

Source
  • staphylococcus aureus (bacteria)
KeywordsHYDROLASE / caseinolytic protease / allosteric regulation / extended conformation / closed state / activator complex / open state

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