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PDBsum entry 3q7h
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PDB id:
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Hydrolase
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Title:
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Structure of the clpp subunit of the atp-dependent clp protease from coxiella burnetii
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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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Coxiella burnetii. Organism_taxid: 360115. Strain: rsa 493. Gene: clpp, coxbursa331_a1213. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.50Å
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R-factor:
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0.172
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R-free:
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0.208
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Authors:
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S.M.Anderson,Z.Wawrzak,E.Gordon,J.Hasseman,W.F.Anderson,A.Savchenko, Center For Structural Genomics Of Infectious Diseases (Csgid)
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Key ref:
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S.M.Anderson
et al.
Structure of the clpp subunit of the ATP-Dependent cl protease from coxiella burnetii.
To be published,
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Date:
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04-Jan-11
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Release date:
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12-Jan-11
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PROCHECK
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Headers
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References
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Q83DJ2
(CLPP_COXBU) -
ATP-dependent Clp protease proteolytic subunit from Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
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Seq:
Struc:
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195 a.a.
186 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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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
