3v5i

X-ray diffraction
2.8Å resolution

The crystal structure of the mutant ClpP S98A (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).
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetradecamer (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, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b
Length: 203 amino acids
Theoretical weight: 22.56 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 97.55Å b: 109.73Å c: 171.41Å
α: 73.1° β: 78.68° γ: 71.46°
R-values:
R R work R free
0.217 0.216 0.242
Expression system: Escherichia coli BL21(DE3)