Roszak Aleksander W, Gardiner Alastair T, Isaacs Neil W, Cogdell Richard J
Department of Chemistry, WestCHEM.
Biochemistry. 2007 Mar 20;46(11):2909-16. doi: 10.1021/bi062154i. Epub 2007 Feb 23.
This study describes the use of brominated phospholipids to distinguish between lipid and detergent binding sites on the surface of a typical alpha-helical membrane protein. Reaction centers isolated from Rhodobacter sphaeroides were cocrystallized with added brominated phospholipids. X-ray structural analysis of these crystals has revealed the presence of two lipid binding sites from the characteristic strong X-ray scattering from the bromine atoms. These results demonstrate the usefulness of this approach to mapping lipid binding sites at the surface of membrane proteins.
本研究描述了使用溴化磷脂来区分典型α-螺旋膜蛋白表面的脂质结合位点和去污剂结合位点。从球形红细菌中分离出的反应中心与添加的溴化磷脂共结晶。对这些晶体的X射线结构分析揭示了由于溴原子具有特征性的强X射线散射而存在两个脂质结合位点。这些结果证明了这种方法在绘制膜蛋白表面脂质结合位点方面的实用性。