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Structure paper

TitleAllosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies
Journal, issue, pagesJ. Bacteriol., Vol. 191, Page 1456-1462, Year 2009
Publish dateJul 9, 2008 (structure data deposition date)
AuthorsLiebscher, M. / Roujeinikova, A.
External linksJ. Bacteriol. / PubMed:19103929
MethodsX-ray diffraction
Resolution2.1 - 2.6 Å
Structure data

PDB-3dpo:
Crystal structure of the substrate binding domain of E. coli DnaK in complex with a short pyrrhocoricin-derived inhibitor peptide
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3dpp:
Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form A)
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3dpq:
Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form B)
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsChaperone / Peptide Binding Protein / molecular chaperone / dnaK / Hsp70 / substrate-binding domain / pyrrhocoricin inhibitor / ATP-binding / Cytoplasm / DNA replication / Membrane / Nucleotide-binding / Phosphoprotein / Stress response

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