Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies▿
| Autor: | Markus Liebscher, Anna Roujeinikova |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Allosteric regulation Molecular Sequence Data Peptide Crystallography X-Ray Microbiology Binding Competitive Structural Biology Heat shock protein Escherichia coli Animals HSP70 Heat-Shock Proteins Amino Acid Sequence Binding site Molecular Biology Peptide sequence chemistry.chemical_classification Binding Sites biology Escherichia coli Proteins Biochemistry chemistry Chaperone (protein) biology.protein Biophysics Insect Proteins Protein folding Linker Allosteric Site Antimicrobial Cationic Peptides Molecular Chaperones |
| Popis: | 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 β-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. |
| Databáze: | OpenAIRE |
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