› 4lj8

X-ray diffraction
2.1Å resolution

ClpB NBD2 R621Q from T. thermophilus in complex with ADP

Released:
DOI: 10.2210/pdb4lj8/pdb
PDB entry 4lj8 coloured by chain, front view.
PDB entry 4lj8 coloured by chain, side view.
PDB entry 4lj8 coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor.
Zeymer C, Barends TR, Werbeck ND, Schlichting I, Reinstein J
OpenAccess logo Acta Crystallogr D Biol Crystallogr 70 582-95 (2014)
PMID: 24531492

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-576823 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein ClpB Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 38.33 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RA63 (Residues: 520-854; Coverage: 39%)
Gene names: TTHA1487, clpB
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: SLS BEAMLINE X10SA
Spacegroup: P65
Unit cell:
a: 74.3Å b: 74.3Å c: 119.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.233
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.
Duran et al. (2017)
2 more

1 mention without citation

Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor.
Zeymer et al. (2014)