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PDBsum entry 3dpp
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Chaperone, peptide binding protein
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PDB id
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3dpp
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References listed in PDB file
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Key reference
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Title
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Allosteric coupling between the lid and interdomain linker in dnak revealed by inhibitor binding studies.
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Authors
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M.Liebscher,
A.Roujeinikova.
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Ref.
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J Bacteriol, 2009,
191,
1456-1462.
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PubMed id
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Abstract
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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.
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