7eko

Electron Microscopy
3.3Å resolution

CrClpP-S1

Released:
Source organism: Chlamydomonas reinhardtii
Primary publication:
The cryo-EM structure of the chloroplast ClpP complex.
Nat Plants 7 1505-1515 (2021)
PMID: 34782772
Related structures: EMD-31171

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:
hetero pentadecamer (preferred)
PDBe Complex ID:
PDB-CPX-104292 (preferred)
Entry contents:
9 distinct polypeptide molecules
Macromolecules (9 distinct):
ATP-dependent Clp protease proteolytic subunit Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 26.57 KDa
Source organism: Chlamydomonas reinhardtii
UniProt:
  • Canonical: A8INX1 (Residues: 46-283; Coverage: 84%)
Gene name: CHLRE_06g299650v5
Sequence domains: Clp protease
ATP-dependent Clp protease proteolytic subunit Chains: B, D, F
Molecule details ›
Chains: B, D, F
Length: 238 amino acids
Theoretical weight: 25.82 KDa
Source organism: Chlamydomonas reinhardtii
UniProt:
  • Canonical: A8IL21 (Residues: 19-256; Coverage: 93%)
Gene name: CHLRE_12g486100v5
Sequence domains: Clp protease
ATP-dependent Clp protease proteolytic subunit Chains: C, E, G
ATP-dependent Clp protease proteolytic subunit Chains: H, J, M
ATP-dependent Clp protease proteolytic subunit Chain: I
ATP-dependent Clp protease proteolytic subunit Chain: K
ATP-dependent Clp protease proteolytic subunit Chain: L
ATP-dependent Clp protease proteolytic subunit Chain: N
ATP-dependent Clp protease ATP-binding subunit CLPT4, chloroplastic Chain: O

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-31171