Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Netherlands Proteomics Centre, University of Groningen, 9747 AG Groningen, The Netherlands.
J Biol Chem. 2012 Oct 26;287(44):37165-70. doi: 10.1074/jbc.M112.386334. Epub 2012 Sep 4.
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.
我们展示了来自粪肠球菌的信息素受体蛋白 PrgZ 与七肽 cCF10(LVTLVFV)复合物的晶体结构,该七肽用于在接合受体和供体细胞之间进行信号传递。PrgZ 与同源寡肽结合蛋白(AppA 和 OppA)的比较解释了 PrgZ 对疏水性七肽的高特异性,而同源蛋白中肽结合的混杂性。