› 4ezz

X-ray diffraction
2.05Å resolution

Crystal structure of the substrate binding domain of E.coli DnaK in complex with the designer peptide ELPLVKI

Released:
DOI: 10.2210/pdb4ezz/pdb
PDB entry 4ezz coloured by chain, front view.
PDB entry 4ezz coloured by chain, side view.
PDB entry 4ezz coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK.
Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Sträter N
J Mol Biol 425 2463-79 (2013)
PMID: 23562829

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero octamer
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141460 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperone protein DnaK Chain: A
Molecule details ›
Chain: A
Length: 219 amino acids
Theoretical weight: 23.82 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6Y8 (Residues: 389-607; Coverage: 34%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Sequence domains: Hsp70 protein
Structure domains:
synthetic peptide ELPLVKI Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 812 Da
Source organism: Escherichia coli K-12
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I222
Unit cell:
a: 93.711Å b: 116.593Å c: 37.056Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.218 0.308
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

12 review citations

Hsp70 chaperone dynamics and molecular mechanism.
Mayer MP. (2013)
11 more

1 mention without citation

Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism.
Wang et al. (2022)