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Structure paper

TitleStructural studies of DnaK in complex with proline rich antimicrobial peptides reveal two different peptide binding modes
Journal, issue, pagesTo be Published
Publish dateMay 3, 2012 (structure data deposition date)
AuthorsZahn, M. / Straeter, N.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.9 - 2.1 Å
Structure data

PDB-4ezs:
Crystal structure of the substrate binding domain of E.coli DnaK in complex with metchnikowin (residues 20 to 26)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4ezu:
Crystal structure of the substrate binding domain of E.coli DnaK in complex with PR-bombesin in space group I222
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4ezv:
Crystal structure of the substrate binding domain of E.coli DnaK in complex with PR-bombesin in space group P21212
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • drosophila melanogaster (fruit fly)
  • bombina maxima (large-webbed bell toad)
KeywordsCHAPERONE/PEPTIDE BINDING PROTEIN / chaperone / peptide binding / CHAPERONE-PEPTIDE BINDING PROTEIN complex

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