3DPQ

Crystal structure of the substrate binding domain of E. coli DnaK in complex with a long pyrrhocoricin-derived inhibitor peptide (form B)

Summary for 3DPQ

• Entry DOI: 10.2210/pdb3dpq/pdb
• Descriptor: Chaperone protein dnaK, inhibitor peptide, SULFATE ION, ... (4 entities in total)
• Functional Keywords: molecular chaperone, dnak, hsp70, substrate-binding domain, pyrrhocoricin inhibitor, atp-binding, chaperone, cytoplasm, dna replication, membrane, nucleotide-binding, phosphoprotein, stress response, peptide binding protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A6Y8
• Total number of polymer chains: 8
• Total formula weight: 105246.85

Authors

Roujeinikova, A. (deposition date: 2008-07-09, release date: 2009-03-10, Last modification date: 2024-11-13)

Primary citation

Liebscher, M.,Roujeinikova, A.
Allosteric coupling between the lid and interdomain linker in DnaK revealed by inhibitor binding studies.
J.Bacteriol., 191:1456-1462, 2009

PubMed Abstract: The molecular chaperone DnaK assists protein folding and refolding, translocation across membranes, and regulation of the heat shock response. In Escherichia coli, the protein is a target for insect-derived antimicrobial peptides, pyrrhocoricins. We present here the X-ray crystallographic analysis of the E. coli DnaK substrate-binding domain in complex with pyrrhocoricin-derived peptide inhibitors. The structures show that pyrrhocoricins act as site-specific, dual-mode (competitive and allosteric) inhibitors, occupying the substrate-binding tunnel and disrupting the latch between the lid and the beta-sandwich. Our structural analysis revealed an allosteric coupling between the movements of the lid and the interdomain linker, identifying a previously unknown mechanism of the lid-mediated regulation of the chaperone cycle.

PubMed: 19103929
DOI: 10.1128/JB.01131-08

Experimental method

X-RAY DIFFRACTION (2.6 Å)