› 1yt2

X-ray diffraction
3.25Å resolution

Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL

Released:
DOI: 10.2210/pdb1yt2/pdb
PDB entry 1yt2 coloured by chain, front view.
PDB entry 1yt2 coloured by chain, side view.
PDB entry 1yt2 coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change.
Dollins DE, Immormino RM, Gewirth DT
J Biol Chem 280 30438-47 (2005)
PMID: 15951571

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmin Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 31.06 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41148 (Residues: 69-337; Coverage: 34%)
Gene names: GRP94, HSP90B1, HSPC4, TRA1
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand PG4 4 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 90.321Å b: 100.257Å c: 64.013Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.252 0.293
Expression system: Escherichia coli BL21(DE3)

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Citations

17 review citations

Structure and mechanism of the Hsp90 molecular chaperone machinery.
Pearl et al. (2006)
16 more

3 mentions without citation

Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer.
Morra et al. (2009)
2 more