8xn4

Electron Microscopy
2.34Å resolution

Cryo-EM structure of the ClpP degradation system in Streptomyces hawaiiensis

Released:
Source organism: Streptomyces hawaiiensis
Primary publication:
Structural insights into the Clp protein degradation machinery.
mBio e0003124 (2024)
PMID: 38501868
Related structures: EMD-38497

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:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetradecamer (preferred)
PDBe Complex ID:
PDB-CPX-242121 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 210 amino acids
Theoretical weight: 22.63 KDa
Source organism: Streptomyces hawaiiensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A5B9BGY8 (Residues: 31-219; Coverage: 86%)
Gene names: CEB94_14110, clpP, clpP1
Sequence domains: Clp protease
ATP-dependent Clp protease proteolytic subunit Chains: H, I, J, K, L, M, N
Molecule details ›
Chains: H, I, J, K, L, M, N
Length: 220 amino acids
Theoretical weight: 24.04 KDa
Source organism: Streptomyces hawaiiensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A5B9BIX9 (Residues: 52-235; Coverage: 78%)
Gene names: CEB94_14105, clpP, clpP2
Sequence domains: Clp protease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.34Å
Relevant EMDB volumes: EMD-38497
Expression system: Escherichia coli BL21(DE3)