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. 2012 Oct 26;287(44):37165-70.
doi: 10.1074/jbc.M112.386334. Epub 2012 Sep 4.

Structure and mode of peptide binding of pheromone receptor PrgZ

Ronnie P-A Berntsson  1 , Gea K Schuurman-Wolters, Gary Dunny, Dirk-Jan Slotboom, Bert Poolman
Affiliations

Structure and mode of peptide binding of pheromone receptor PrgZ

Ronnie P-A Berntsson et al. J Biol Chem. .

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.

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Figures

FIGURE 1.
FIGURE 1.
A, hydrogen-bonding network forming the binding site for cCF10 (pink) within PrgZ* (teal). B, schematic representation of PrgZ*, with the bound cCF10 ligand in orange and the binding cavity outlined in gray mesh.
FIGURE 2.
FIGURE 2.
DSC scans of PrgZ* without ligand (solid black line), with cCF10 added (dotted blue line), and with iCF10 added (dashed red line). The Tm of each measurement is indicated above each peak.
See this image and copyright information in PMC

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