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PDBsum entry 3hln

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protein metals Protein-protein interface(s) links
Hydrolase PDB id
3hln
Jmol
Contents
Protein chains
(+ 22 more) 162 a.a. *
Metals
_CA ×13
* Residue conservation analysis
PDB id:
3hln
Name: Hydrolase
Title: Crystal structure of clpp a153c mutant with inter-heptamer d bonds
Structure: Atp-dependent clp protease proteolytic subunit. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r v, w, x, y, z, 1, 2. Fragment: unp residues 15-207. Synonym: endopeptidase clp, caseinolytic protease, protease shock protein f21.5. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k-12. Gene: b0437, clpp, jw0427, lopp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
3.20Å     R-factor:   0.215     R-free:   0.253
Authors: M.S.Kimber,A.Y.H.Yu,M.Borg,H.S.Chan,W.A.Houry
Key ref: M.S.Kimber et al. (2010). Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure, 18, 798-808. PubMed id: 20637416
Date:
27-May-09     Release date:   28-Jul-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A6G7  (CLPP_ECOLI) -  ATP-dependent Clp protease proteolytic subunit
Seq:
Struc:
207 a.a.
162 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.92  - Endopeptidase Clp.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 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).
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   3 terms 
  Biological process     response to stress   5 terms 
  Biochemical function     hydrolase activity     5 terms  

 

 
Structure 18:798-808 (2010)
PubMed id: 20637416  
 
 
Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.
M.S.Kimber, A.Y.Yu, M.Borg, E.Leung, H.S.Chan, W.A.Houry.
 
  ABSTRACT  
 
No abstract given.