8e91

Electron Microscopy
2.57Å resolution

Cryo-EM structure of substrate-free ClpX.ClpP

Released:
Source organism: Escherichia coli
Related structures: EMD-27952

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:
hetero icosamer (preferred)
PDBe Complex ID:
PDB-CPX-141328 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent Clp protease ATP-binding subunit ClpX Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 424 amino acids
Theoretical weight: 46.41 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H1 (Residues: 1-424; Coverage: 100%)
Gene names: JW0428, b0438, clpX, lopC
Sequence domains:
ATP-dependent Clp protease proteolytic subunit Chains: H, I, J, K, L, M, N, h, i, j, k, l, m, n
Molecule details ›
Chains: H, I, J, K, L, M, N, h, i, j, k, l, m, n
Length: 207 amino acids
Theoretical weight: 23.47 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6G7 (Residues: 16-207; Coverage: 93%)
Gene names: JW0427, b0437, clpP, lopP
Sequence domains: Clp protease

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.57Å
Relevant EMDB volumes: EMD-27952
Expression system: Escherichia coli