Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein.
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.
Smith
V F
VF
Department of Biochemistry and Biophysics, Washinton State University, Pullman 99164-4660, USA.
Hardy
S J
SJ
Randall
L L
LL
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D029968:Escherichia coli Proteins; D006868:Hydrolysis; D008024:Ligands; D008074:Lipoproteins / Q000737:chemistry / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D010455:Peptides / Q000302:isolation & purification / Q000378:metabolism; D011485:Protein Binding
D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008024:Ligands; D008074:Lipoproteins; D018832:Molecular Chaperones; C499290:OppA protein, E coli; D010455:Peptides; C057842:SecB protein, Bacteria; C046506:oligopeptide-binding protein, bacteria