5vz2

X-ray diffraction
2.26Å resolution

Structure of ClpP from Staphylococcus aureus in complex with Acyldepsipeptide

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:
hetero 28-mer (preferred)
PDBe Complex ID:
PDB-CPX-166238 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G, I, K, L, M, N, S, T
Molecule details ›
Chains: A, B, C, D, E, F, G, I, K, L, M, N, S, T
Length: 203 amino acids
Theoretical weight: 22.61 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
Acyldepsipeptide Chains: H, J, O, P, Q, R, U, V, X, Y, Z, a, b, c
Molecule details ›
Chains: H, J, O, P, Q, R, U, V, X, Y, Z, a, b, c
Length: 7 amino acids
Theoretical weight: 725 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 94.562Å b: 126.131Å c: 145.794Å
α: 90° β: 93.42° γ: 90°
R-values:
R R work R free
0.18 0.179 0.219
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided