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Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide‐binding protein
Author(s) -
Smith Virginia F.,
Randall Linda L.,
Hardy SIMON J. S.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060815
Subject(s) - oligopeptide , chaperone (clinical) , chemistry , biophysics , ligand (biochemistry) , biochemistry , microbiology and biotechnology , biology , peptide , receptor , medicine , pathology
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 ∼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.