› 4jne

X-ray diffraction
1.96Å resolution

Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP

Released:
DOI: 10.2210/pdb4jne/pdb
PDB entry 4jne coloured by chain, front view.
PDB entry 4jne coloured by chain, side view.
PDB entry 4jne coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP.
Qi R, Sarbeng EB, Liu Q, Le KQ, Xu X, Xu H, Yang J, Wong JL, Vorvis C, Hendrickson WA, Zhou L, Liu Q
Nat Struct Mol Biol 20 900-7 (2013)
PMID: 23708608

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-141465 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein DnaK Chains: A, B
Molecule details ›
Chains: A, B
Length: 608 amino acids
Theoretical weight: 65.89 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6Y8 (Residues: 2-610; Coverage: 95%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand ATP 2 x ATP
Ligand SO4 11 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: I422
Unit cell:
a: 290.678Å b: 290.678Å c: 99.317Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

37 review citations

In vivo aspects of protein folding and quality control.
Balchin et al. (2016)
36 more

30 mentions without citation

Hsp70 chaperone: a master player in protein homeostasis.
Fernández-Fernández et al. (2018)
29 more