title: Peptide binding by chaperone SecB: implications for recognition of nonnative structure.
abstract: The molecular basis for recognition of nonnative proteins by the molecular chaperone SecB was investigated with an in vitro assay based on the protection of SecB from proteolysis when a ligand is bound. The SecB tetramer has multiple binding sites for positively charged peptides. When the peptide binding sites are occupied, the complex undergoes a conformational change to expose hydrophobic sites that bind the fluorescent probe 1-anilinonaphthalene-8-sulfonate. A model is proposed for interaction of nonnative polypeptides with both hydrophilic and hydrophobic sites on SecB.
authors.affiliation: Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.
authors.forename: L L
authors.initials: LL
authors.lastname: Randall
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D066298:In Vitro Techniques; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009994:Osmolar Concentration; D010455:Peptides / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; C057842:SecB protein, Bacteria