› 1usv

X-ray diffraction
2.7Å resolution

The Structure of the complex between Aha1 and HSP90

Released:
DOI: 10.2210/pdb1usv/pdb
PDB entry 1usv coloured by chain, front view.
PDB entry 1usv coloured by chain, side view.
PDB entry 1usv coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.
Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH
EMBO J 23 1402-10 (2004)
PMID: 15039704

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136255 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent molecular chaperone HSP82 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 260 amino acids
Theoretical weight: 30.5 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 271-530; Coverage: 37%)
Gene names: HSP82, HSP90, YPL240C
Sequence domains: Hsp90 protein
Structure domains:
Hsp90 co-chaperone AHA1 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 170 amino acids
Theoretical weight: 19.12 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12449 (Residues: 1-156; Coverage: 45%)
Gene names: AHA1, YD8142.16, YD8142B.06, YDR214W
Sequence domains: Activator of Hsp90 ATPase, N-terminal
Structure domains: Activator of Hsp90 ATPase Aha1, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 58.397Å b: 207.93Å c: 84.447Å
α: 90° β: 97.68° γ: 90°
R-values:
R R work R free
0.229 0.229 0.298
Expression system: Escherichia coli

Quick links

Citations

28 review citations

Targeting the dynamic HSP90 complex in cancer.
Trepel et al. (2010)
27 more

8 mentions without citation

Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.
Koulov et al. (2010)
7 more