› 3hte

X-ray diffraction
4.03Å resolution

Crystal structure of nucleotide-free hexameric ClpX

Released:
DOI: 10.2210/pdb3hte/pdb
PDB entry 3hte coloured by chain, front view.
PDB entry 3hte coloured by chain, side view.
PDB entry 3hte coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Glynn SE, Martin A, Nager AR, Baker TA, Sauer RT
Cell 139 744-56 (2009)
PMID: 19914167

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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: 363 amino acids
Theoretical weight: 39.43 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H1 (Residues: 62-424; Coverage: 86%)
Gene names: JW0428, b0438, clpX, lopC
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 63.325Å b: 199.917Å c: 202.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.279 0.278 0.313
Expression system: Escherichia coli

Quick links

Citations

48 review citations

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

11 mentions without citation

Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Glynn et al. (2009)
10 more