› 3a6m

X-ray diffraction
3.23Å resolution

Crystal structure of GrpE from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb3a6m/pdb
PDB entry 3a6m coloured by chain, front view.
PDB entry 3a6m coloured by chain, side view.
PDB entry 3a6m coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure of a thermophilic GrpE protein: insight into thermosensing function for the DnaK chaperone system.
Nakamura A, Takumi K, Miki K
J Mol Biol 396 1000-11 (2010)
PMID: 20036249

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-176337 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein GrpE Chains: A, B
Molecule details ›
Chains: A, B
Length: 177 amino acids
Theoretical weight: 20.06 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56236 (Residues: 1-177; Coverage: 100%)
Gene names: TTHA1490, grpE
Sequence domains: GrpE
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P4332
Unit cell:
a: 210.382Å b: 210.382Å c: 210.382Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.238
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Burmann et al. (2015)
1 more

5 mentions without citation

Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates.
Karunanayake et al. (2021)
4 more