Purification and characterization of a periplasmic oligopeptide binding protein from Escherichia coli.

Guyer CA, Morgan DG, Osheroff N, Staros JV
J Biol Chem. 1985 260 (19): 10812-8

PMID: 3897225

We have purified and characterized an oligopeptide binding protein released from the periplasm of Escherichia coli W by mild osmotic shock. The purified protein was greater than 97% homogeneous as determined by either sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Mr = 60,000) or isoelectric focusing (pI = 5.95). The binding protein has a Stokes radius of 30 A and a sedimentation coefficient (s(0)20,w) of 4.6 S. Based on these hydrodynamic studies, the native protein has a molecular weight of 56,000. The tripeptide, Ala-Phe-[3H]Gly, which is transported via the shock-sensitive sensitive oligopeptide permease, binds to the purified protein in dilute solution with a Kd of 0.1 microM and a stoichiometry of approximately 1 to 1. Results from this study support the hypothesis that this periplasmic oligopeptide binding protein functions in the initial recognition of peptide substrates for the oligopeptide permease system.

MeSH Terms (12)

Bacterial Proteins Carrier Proteins Chromatography, DEAE-Cellulose Chromatography, Gel Electrophoresis, Polyacrylamide Gel Escherichia coli Escherichia coli Proteins Kinetics Lipoproteins Molecular Weight Oligopeptides Protein Conformation

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