› 2iop

X-ray diffraction
3.55Å resolution

Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP

Released:
DOI: 10.2210/pdb2iop/pdb
PDB entry 2iop coloured by chain, front view.
PDB entry 2iop coloured by chain, side view.
PDB entry 2iop 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

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-141496 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein HtpG Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 78.618Å b: 145.06Å c: 165.352Å
α: 90° β: 92.43° γ: 90°
R-values:
R R work R free
0.317 0.317 0.357
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

58 review citations

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

28 mentions without citation

Conformational dynamics of the molecular chaperone Hsp90.
Krukenberg et al. (2011)
27 more