2fzs

X-ray diffraction
1.9Å resolution

Crystal structure of E. coli ClpP with a Peptide Chloromethyl Ketone Covalently Bound at the Active Site

Released:
Source organism: Escherichia coli

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
PDBe Complex ID:
PDB-CPX-141326 (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: 193 amino acids
Theoretical weight: 21.59 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6G7 (Residues: 15-207; Coverage: 93%)
Gene names: JW0427, b0437, clpP, lopP
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: NSLS BEAMLINE X9B
Spacegroup: C2
Unit cell:
a: 190.7Å b: 101Å c: 155.4Å
α: 90° β: 99° γ: 90°
R-values:
R R work R free
0.176 0.173 0.233
Expression system: Escherichia coli BL21(DE3)