7feq

Electron Microscopy
3.2Å resolution

Cryo-EM structure of apo BsClpP at pH 6.5

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 tetradecamer (preferred)
PDBe Complex ID:
PDB-CPX-160369 (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: 202 amino acids
Theoretical weight: 22.4 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P80244 (Residues: 2-197; Coverage: 100%)
Gene names: BSU34540, clpP, yvdN
Sequence domains: Clp protease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.2Å
Relevant EMDB volumes: EMD-31560
Expression system: Escherichia coli