› 4cgq

X-ray diffraction
2Å resolution

Full length Tah1 bound to HSP90 peptide SRMEEVD

Released:
DOI: 10.2210/pdb4cgq/pdb
PDB entry 4cgq coloured by chain, front view.
PDB entry 4cgq coloured by chain, side view.
PDB entry 4cgq coloured by chain, top view.
Source organisms:
Primary publication:
Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes.
Morgan RM, Pal M, Roe SM, Pearl LH, Prodromou C
Acta Crystallogr D Biol Crystallogr 71 1197-206 (2015)
PMID: 25945584

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139818 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
TPR repeat-containing protein associated with Hsp90 Chain: A
Molecule details ›
Chain: A
Length: 111 amino acids
Theoretical weight: 12.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P25638 (Residues: 1-111; Coverage: 100%)
Gene names: TAH1, YCR060W, YCR60W
Sequence domains: Tetratricopeptide repeat
Heat shock protein HSP 90-alpha Chain: Q
Molecule details ›
Chain: Q
Length: 7 amino acids
Theoretical weight: 866 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P07900 (Residues: 726-732; Coverage: 1%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 62.79Å b: 62.79Å c: 57.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.21
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Review: The HSP90 molecular chaperone-an enigmatic ATPase.
Pearl LH. (2016)
2 more

2 mentions without citation

Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes.
Morgan et al. (2015)
1 more