› 2cg9

X-ray diffraction
3.1Å resolution

Crystal structure of an Hsp90-Sba1 closed chaperone complex

Released:
DOI: 10.2210/pdb2cg9/pdb
PDB entry 2cg9 coloured by chain, front view.
PDB entry 2cg9 coloured by chain, side view.
PDB entry 2cg9 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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136259 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent molecular chaperone HSP82 Chains: A, B
Molecule details ›
Chains: A, B
Length: 677 amino acids
Theoretical weight: 78.08 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02829 (Residues: 1-677; Coverage: 96%)
Gene names: HSP82, HSP90, YPL240C
Sequence domains:
Structure domains:
Co-chaperone protein SBA1 Chains: X, Y
Molecule details ›
Chains: X, Y
Length: 134 amino acids
Theoretical weight: 15.77 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28707 (Residues: 2-135; Coverage: 62%)
Gene names: SBA1, YKL117W, YKL518
Structure domains: Immunoglobulin-like

Ligands and Environments

1 bound ligand:
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41212
Unit cell:
a: 126.729Å b: 126.729Å c: 279.777Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.314 0.312 0.353
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

93 review citations

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

171 mentions without citation

Chaperone machines for protein folding, unfolding and disaggregation.
Saibil H. (2013)
170 more