› 4hse

X-ray diffraction
2.2Å resolution

Crystal structure of ClpB NBD1 in complex with guanidinium chloride and ADP

Released:
DOI: 10.2210/pdb4hse/pdb
PDB entry 4hse coloured by chain, front view.
PDB entry 4hse coloured by chain, side view.
PDB entry 4hse coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride.
Zeymer C, Werbeck ND, Schlichting I, Reinstein J
J Biol Chem 288 7065-76 (2013)
PMID: 23341453

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-193125 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein ClpB Chain: A
Molecule details ›
Chain: A
Length: 397 amino acids
Theoretical weight: 45.04 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RA63 (Residues: 142-534; Coverage: 46%)
Gene names: TTHA1487, clpB
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand GAI 1 x GAI
Ligand ADP 1 x ADP
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3121
Unit cell:
a: 60.99Å b: 60.99Å c: 213.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.225 0.266
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation.
Mogk et al. (2015)
3 more

5 mentions without citation

Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase.
Deville et al. (2017)
4 more