› 6pp5

Electron Microscopy
3.98Å resolution

ClpX in ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 4

Released:
DOI: 10.2210/pdb6pp5/pdb
PDB entry 6pp5 coloured by chain, front view.
PDB entry 6pp5 coloured by chain, side view.
PDB entry 6pp5 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate.
Fei X, Bell TA, Jenni S, Stinson BM, Baker TA, Harrison SC, Sauer RT
Elife 9 (2020)
PMID: 32108573
Related structures: EMD-20419

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141345 (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: 369 amino acids
Theoretical weight: 39.84 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H1 (Residues: 62-424; Coverage: 86%)
Gene names: JW0428, b0438, clpX, lopC
Sequence domains:
substrate peptide Chain: S
Molecule details ›
Chain: S
Length: 12 amino acids
Theoretical weight: 1.04 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand AGS 5 x AGS
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.98Å
Relevant EMDB volumes: EMD-20419
Expression system: Escherichia coli

Quick links

Citations

19 review citations

The molecular principles governing the activity and functional diversity of AAA+ proteins.
Puchades et al. (2020)
18 more

3 mentions without citation

Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.
Izert et al. (2021)
2 more