3qwd

X-ray diffraction
2.1Å resolution

Crystal structure of ClpP from Staphylococcus aureus

Released:
Primary publication:
A conformational switch underlies ClpP protease function.
Angew Chem Int Ed Engl 50 5749-52 (2011)
PMID: 21544912

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

Assemblies composition:
homo tetradecamer
homo heptamer (preferred)
PDBe Complex ID:
PDB-CPX-173495 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 203 amino acids
Theoretical weight: 22.58 KDa
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2G036 (Residues: 1-195; Coverage: 100%)
Gene names: SAOUHSC_00790, clpP
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 172.048Å b: 177.974Å c: 100.278Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.226
Expression system: Escherichia coli BL21(DE3)