3st9

X-ray diffraction
2.43Å resolution

Crystal structure of ClpP in heptameric form from Staphylococcus aureus

Released:

Function and Biology Details

Reaction catalysed:
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 hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
PDBe Complex ID:
PDB-CPX-159118 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 197 amino acids
Theoretical weight: 21.68 KDa
Source organism: Staphylococcus aureus subsp. aureus MW2
Expression system: Escherichia coli
UniProt:
  • Canonical: P63786 (Residues: 1-195; Coverage: 100%)
Gene names: MW0730, clpP
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P6122
Unit cell:
a: 121.289Å b: 121.289Å c: 404.377Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.239 0.271
Expression system: Escherichia coli