› 2o1w

X-ray diffraction
3.4Å resolution

Structure of N-terminal plus middle domains (N+M) of GRP94

Released:
DOI: 10.2210/pdb2o1w/pdb
PDB entry 2o1w coloured by chain, front view.
PDB entry 2o1w coloured by chain, side view.
PDB entry 2o1w coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.
Dollins DE, Warren JJ, Immormino RM, Gewirth DT
Mol Cell 28 41-56 (2007)
PMID: 17936703

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmin Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 506 amino acids
Theoretical weight: 58.18 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41148 (Residues: 73-594; Coverage: 62%)
Gene names: GRP94, HSP90B1, HSPC4, TRA1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 210.33Å b: 137.5Å c: 133.15Å
α: 90° β: 124.1° γ: 90°
R-values:
R R work R free
0.315 0.314 0.332
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

45 review citations

HSP90 at the hub of protein homeostasis: emerging mechanistic insights.
Taipale et al. (2010)
44 more

1 mention without citation

The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis.
Cunningham et al. (2012)