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Structure and Mode of Peptide Binding of Pheromone Receptor PrgZ |
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| Authors: | Ronnie P.-A. Berntsson Gea K. Schuurman-Wolters Gary Dunny Dirk-Jan Slotboom Bert Poolman |
| Affiliation: | From the ‡Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Netherlands Proteomics Centre, and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands and ;the §Department of Microbiology, University of Minnesota, Minneapolis, Minnesota 55455 |
| Abstract: | We present the crystal structure of the pheromone receptor protein PrgZ from Enterococcus faecalis in complex with the heptapeptide cCF10 (LVTLVFV), which is used in signaling between conjugative recipient and donor cells. Comparison of PrgZ with homologous oligopeptide-binding proteins (AppA and OppA) explains the high specificity of PrgZ for hydrophobic heptapeptides versus the promiscuity of peptide binding in the homologous proteins. |
| Keywords: | ABC Transporter Bacterial Conjugation Bacterial Signal Transduction Membrane Transport Pheromone Receptor Structure-Function |