› 1ksf

X-ray diffraction
2.6Å resolution

Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains

Released:
DOI: 10.2210/pdb1ksf/pdb
PDB entry 1ksf coloured by chain, front view.
PDB entry 1ksf coloured by chain, side view.
PDB entry 1ksf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.
Guo F, Maurizi MR, Esser L, Xia D
J Biol Chem 277 46743-52 (2002)
PMID: 12205096

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease ATP-binding subunit ClpA Chain: X
Molecule details ›
Chain: X
Length: 758 amino acids
Theoretical weight: 84.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABH9 (Residues: 1-758; Coverage: 100%)
Gene names: JW0866, b0882, clpA, lopD
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 2 x MG
Ligand MET 1 x MET
Ligand PGE 2 x PGE
Ligand ADP 2 x ADP
Ligand IPA 5 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P65
Unit cell:
a: 124.107Å b: 124.107Å c: 97.042Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.216 0.304
Expression system: Escherichia coli

Quick links

Citations

30 review citations

Proteasomes and their kin: proteases in the machine age.
Pickart et al. (2004)
29 more

11 mentions without citation

The AAA+ superfamily of functionally diverse proteins.
Snider et al. (2008)
10 more