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Structure paper

TitleClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores.
Journal, issue, pagesCommun Biol, Vol. 2, Page 410-410, Year 2019
Publish dateDec 5, 2018 (structure data deposition date)
AuthorsMabanglo, M.F. / Leung, E. / Vahidi, S. / Seraphim, T.V. / Eger, B.T. / Bryson, S. / Bhandari, V. / Zhou, J.L. / Mao, Y.Q. / Rizzolo, K. ...Mabanglo, M.F. / Leung, E. / Vahidi, S. / Seraphim, T.V. / Eger, B.T. / Bryson, S. / Bhandari, V. / Zhou, J.L. / Mao, Y.Q. / Rizzolo, K. / Barghash, M.M. / Goodreid, J.D. / Phanse, S. / Babu, M. / Barbosa, L.R.S. / Ramos, C.H.I. / Batey, R.A. / Kay, L.E. / Pai, E.F. / Houry, W.A.
External linksCommun Biol / PubMed:31925204
MethodsX-ray diffraction
Resolution1.9 - 2.7 Å
Structure data

PDB-6nah:
Crystal structure of Neisseria meningitidis ClpP protease in complex with Acyldepsipeptide-14 (ADEP-14)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-6naq:
Crystal structure of Neisseria meningitidis ClpP protease in Apo form
Method: X-RAY DIFFRACTION / Resolution: 2.022 Å

PDB-6naw:
Crystal structure of Neisseria meningitidis ClpP E58A activated mutant
Method: X-RAY DIFFRACTION / Resolution: 2.399 Å

PDB-6nay:
Crystal structure of Neisseria meningitidis ClpP protease E31A+E58A activated double mutant
Method: X-RAY DIFFRACTION / Resolution: 2.199 Å

PDB-6nb1:
Crystal structure of Escherichia coli ClpP protease complexed with small molecule activator, ACP1-06
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-OCA:
OCTANOIC ACID (CAPRYLIC ACID)

ChemComp-HOH:
WATER

ChemComp-K:
Unknown entry

ChemComp-KHS:
N-{2-[(2-chlorophenyl)sulfanyl]ethyl}-2-methyl-2-{[5-(trifluoromethyl)pyridin-2-yl]sulfonyl}propanamide

ChemComp-GOL:
GLYCEROL

Source
  • neisseria meningitidis (bacteria)
  • synthetic construct (others)
  • escherichia coli (strain k12) (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / Serine protease / antibiotic / anticancer / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex

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