› 1um8

X-ray diffraction
2.6Å resolution

Crystal structure of helicobacter pylori ClpX

Released:
DOI: 10.2210/pdb1um8/pdb
PDB entry 1um8 coloured by chain, front view.
PDB entry 1um8 coloured by chain, side view.
PDB entry 1um8 coloured by chain, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
Crystal structure of ClpX molecular chaperone from Helicobacter pylori.
Kim DY, Kim KK
J Biol Chem 278 50664-70 (2003)
PMID: 14514695

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease ATP-binding subunit ClpX Chain: A
Molecule details ›
Chain: A
Length: 376 amino acids
Theoretical weight: 42.09 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: O25926 (Residues: 71-446; Coverage: 84%)
Gene names: HP_1374, clpX
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU, PAL/PLS BEAMLINE 6B
Spacegroup: P65
Unit cell:
a: 78.515Å b: 78.515Å c: 131.514Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.219 0.258
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

3 mentions without citation

Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.
Li et al. (2010)
2 more