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Solution NMR

SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.

Released:
DOI: 10.2210/pdb1exk/pdb
PDB entry 1exk coloured by chain, ensemble of 20 models, front view.
PDB entry 1exk coloured by chain, ensemble of 20 models, side view.
PDB entry 1exk coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ.
Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ
J Mol Biol 300 805-18 (2000)
PMID: 10891270

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein DnaJ Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08622 (Residues: 131-209; Coverage: 21%)
Gene names: JW0014, b0015, dnaJ, groP
Sequence domains:
Structure domains: Heat shock protein DnaJ, cysteine-rich domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics followed by simulated annealing
Expression system: Escherichia coli

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Citations

7 review citations

Zinc finger proteins: new insights into structural and functional diversity.
Laity et al. (2001)
6 more

10 mentions without citation

Mechanisms for regulation of Hsp70 function by Hsp40.
Fan et al. (2003)
9 more