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PDBsum entry 9irp
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PDB id:
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Hydrolase
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Title:
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Structure of clpp from staphylococcus aureus in complex with zg297
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Structure:
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Atp-dependent clp protease proteolytic subunit. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Synonym: endopeptidase clp. Engineered: yes
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Source:
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Staphylococcus aureus. Organism_taxid: 1280. Gene: clpp_1, clpp, clpp_2, a6760_03845, bn1321_180012, cv021_05845, e1948_01285, e1948_03940, ep54_12650, eq90_03850, faf17_09860, g6w63_01780, g6y24_04455, go793_13920, go814_03290, go942_03115, gqx37_00485, gz156_04030, gz163_03895, h2639_09715, hmpref3211_00508, m1k003_1188, nctc10702_01301, nctc13131_00808, nctc5664_02933, nctc7878_03438, nctc7972_01134, qu38_10910, samea1531744_00638, samea2078260_01084, samea2078588_00822,
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Resolution:
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1.90Å
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R-factor:
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0.175
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R-free:
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0.208
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Authors:
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B.Y.Wei,P.Y.Wang,T.Zhang,C.-G.Yang
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Key ref:
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T.Zhang
et al.
(2024).
Structure-Guided development of selective caseinolyti protease p agonists as antistaphylococcal agents..
Cell rep med,
5,
01837.
PubMed id:
DOI:
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Date:
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16-Jul-24
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Release date:
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23-Oct-24
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PROCHECK
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Headers
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References
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Q2G036
(CLPP_STAA8) -
ATP-dependent Clp protease proteolytic subunit from Staphylococcus aureus (strain NCTC 8325 / PS 47)
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Seq:
Struc:
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195 a.a.
188 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.3.4.21.92
- endopeptidase Clp.
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Reaction:
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Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are cleaved (such as succinyl-Leu-Tyr-|-NHMEC; and Leu-Tyr-Leu-|-Tyr-Trp, in which the cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp- bond also occurs).
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Links
