PMID:9260287

Citation	Smith, VF, Hardy, SJ and Randall, LL (1997) Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein. Protein Sci. 6:1746-55
Abstract	Chaperone proteins demonstrate the paradoxical ability to bind ligands rapidly and with high affinity but with no apparent sequence specificity. To learn more about this singular property, we have mapped the binding frame of the chaperone SecB from E. coli on the oligopeptide-binding protein. Similar studies performed on the maltose-binding and galactose-binding proteins revealed centrally positioned binding frames of approximately 160 aminoacyl residues. The work described here shows that OppA, which is significantly longer than the previously studied ligands, has a binding frame that covers 460 amino acids, nearly the entire length of the protein. We propose modes of binding to account for the data.
Links	PubMed PMC2143767 Online version:10.1002/pro.5560060815
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Escherichia coli Proteins; Hydrolysis; Ligands; Lipoproteins/chemistry; Lipoproteins/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Peptides/isolation & purification; Peptides/metabolism; Protein Binding
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