› 7n6k

X-ray diffraction
2.55Å resolution

Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RALALLPLSR

Released:
DOI: 10.2210/pdb7n6k/pdb
PDB entry 7n6k coloured by chain, front view.
PDB entry 7n6k coloured by chain, side view.
PDB entry 7n6k coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Selective promiscuity in the binding of E. coli Hsp70 to an unfolded protein.
Clerico EM, Pozhidaeva AK, Jansen RM, Özden C, Tilitsky JM, Gierasch LM
Proc Natl Acad Sci U S A 118 (2021)
PMID: 34625496

Function and Biology Details

Reaction catalysed: 
A phosphate monoester + H(2)O = an alcohol + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132768 (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 BL21(DE3)
UniProt:
  • Canonical: P0A6Y8 (Residues: 389-607; Coverage: 34%)
Gene names: JW0013, b0014, dnaK, groP, grpF, seg
Sequence domains: Hsp70 protein
Alkaline phosphatase Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.11 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
UniProt:
  • Canonical: P00634 (Residues: 6-15; Coverage: 0%)
Gene names: JW0374, b0383, phoA

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I222
Unit cell:
a: 37.763Å b: 94.773Å c: 117.109Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.208 0.306
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

3 review citations

Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.
Marszalek et al. (2022)
2 more