› 2cge

X-ray diffraction
3Å resolution

Crystal structure of an Hsp90-Sba1 closed chaperone complex

Released:
DOI: 10.2210/pdb2cge/pdb
PDB entry 2cge coloured by chain, front view.
PDB entry 2cge coloured by chain, side view.
PDB entry 2cge coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.
Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH
Nature 440 1013-7 (2006)
PMID: 16625188

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-136260 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent molecular chaperone HSP82 Chains: A, B, D
Molecule details ›
Chains: A, B, D
Length: 405 amino acids
Theoretical weight: 46.84 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 273-677; Coverage: 57%)
Gene names: HSP82, HSP90, YPL240C
Sequence domains: Hsp90 protein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P43212
Unit cell:
a: 105.555Å b: 105.555Å c: 289.315Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.258 0.257 0.288
Expression system: Escherichia coli

Quick links

Citations

114 review citations

Molecular chaperones in protein folding and proteostasis.
Hartl et al. (2011)
113 more

18 mentions without citation

Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases.
Thomsen et al. (2008)
17 more