› 1ovx

Solution NMR

NMR structure of the E. coli ClpX chaperone zinc binding domain dimer

Released:
DOI: 10.2210/pdb1ovx/pdb
PDB entry 1ovx coloured by chain, front view.
PDB entry 1ovx coloured by chain, side view.
PDB entry 1ovx coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Solution structure of the dimeric zinc binding domain of the chaperone ClpX.
Donaldson LW, Wojtyra U, Houry WA
J Biol Chem 278 48991-6 (2003)
PMID: 14525985

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141341 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease ATP-binding subunit ClpX Chains: A, B
Molecule details ›
Chains: A, B
Length: 67 amino acids
Theoretical weight: 7.75 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A6H1 (Residues: 2-61; Coverage: 14%)
Gene names: JW0428, b0438, clpX, lopC
Sequence domains: ClpX C4-type zinc finger

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing cartesian dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

AAA+ proteases: ATP-fueled machines of protein destruction.
Sauer et al. (2011)
7 more

6 mentions without citation

ClpXP, an ATP-powered unfolding and protein-degradation machine.
Baker et al. (2012)
5 more