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Structure and mode of peptide binding of pheromone receptor PrgZ.

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.

SUBMITTER: Berntsson RP

PROVIDER: S-EPMC3481316 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Structure and mode of peptide binding of pheromone receptor PrgZ.

Berntsson Ronnie P-A RP Schuurman-Wolters Gea K GK Dunny Gary G Slotboom Dirk-Jan DJ Poolman Bert B

The Journal of biological chemistry 20120904 44

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. ...[more]

PMID: 22948145

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