title: Determination of the binding frame within a physiological ligand for the chaperone SecB.
abstract: The hallmark of the class of proteins called chaperones is the amazing ability to bind tightly to a wide array of polypeptide ligands that have no consensus in sequence; chaperones recognize non-native structure. As a step in the elucidation of the molecular mechanism of such remarkable binding, we have characterized complexes between the bacterial chaperone SecB and a series of ligands related to maltose-binding protein. SecB interacts at multiple sites on its polypeptide ligand. The entire binding region covers approximately half of the primary sequence of maltose-binding protein and comprises contiguous sites positioned around the center of the sequence.
authors.affiliation: Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.
authors.forename: T B
authors.initials: TB
authors.lastname: Topping
authors.forename: L L
authors.initials: LL
authors.lastname: Randall
mesh_terms: D018528:ATP-Binding Cassette Transporters; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D008024:Ligands; D008320:Maltose / Q000378:metabolism; D058619:Maltose-Binding Proteins; D015394:Molecular Structure; D008970:Molecular Weight; D009004:Monosaccharide Transport Proteins; D011485:Protein Binding; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism
chemical_list: D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008024:Ligands; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D011498:Protein Precursors; C057842:SecB protein, Bacteria; C461599:maltose transport system, E coli; D008320:Maltose