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Structure paper

TitleThe structure of caseinolytic protease subunit ClpP2 reveals a functional model of the caseinolytic protease system from Chlamydia trachomatis.
Journal, issue, pagesJ. Biol. Chem., Vol. 299, Page 102762-102762, Year 2023
Publish dateJul 7, 2022 (structure data deposition date)
AuthorsAzadmanesh, J. / Seleem, M.A. / Struble, L. / Wood, N.A. / Fisher, D.J. / Lovelace, J.J. / Artigues, A. / Fenton, A.W. / Borgstahl, G.E.O. / Ouellette, S.P. / Conda-Sheridan, M.
External linksJ. Biol. Chem. / PubMed:36463962
MethodsX-ray diffraction
Resolution2.66 Å
Structure data

PDB-8dla:
ClpP2 from Chlamydia trachomatis bound by MAS1-12
Method: X-RAY DIFFRACTION / Resolution: 2.66 Å

Chemicals

ChemComp-UER:
1-{4-[(4-chlorophenyl)methyl]piperazin-1-yl}-2-methyl-2-[5-(trifluoromethyl)pyridine-2-sulfonyl]propan-1-one

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • chlamydia trachomatis (bacteria)
KeywordsHYDROLASE/INHIBITOR / Protease / Chlamydia trachomatis / HYDROLASE / HYDROLASE-INHIBITOR complex

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