› 2ioq

X-ray diffraction
3.5Å resolution

Crystal Structure of full-length HTPG, the Escherichia coli HSP90

Released:
DOI: 10.2210/pdb2ioq/pdb
PDB entry 2ioq coloured by chain, front view.
PDB entry 2ioq coloured by chain, side view.
PDB entry 2ioq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.
Shiau AK, Harris SF, Southworth DR, Agard DA
Cell 127 329-40 (2006)
PMID: 17055434

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141496 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein HtpG Chains: A, B
Molecule details ›
Chains: A, B
Length: 624 amino acids
Theoretical weight: 71.52 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6Z3 (Residues: 1-624; Coverage: 100%)
Gene names: JW0462, b0473, htpG
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P6522
Unit cell:
a: 105.124Å b: 105.124Å c: 531.077Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.329 0.329 0.37
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

52 review citations

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

57 mentions without citation

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