PDF(Pubmed)
Abstract：
Here we report the structure of Opa60 in lipid bilayers using proton-detected magic-angle spinning nuclear magnetic resonance (MAS NMR). Preparations including near-native oligosaccharide lipids reveal a consistent picture of a stable transmembrane beta barrel with a minor increase in the structured region as compared with the previously reported detergent structure. The large variable loops known to interact with host proteins could not be detected, confirming their dynamic nature even in a lipid bilayer environment. The structure provides a starting point for investigation of the functional role of Opa60 in gonococcal infection, which is understood to involve interaction with host proteins. At the same time, it demonstrates the recent advances in proton-detected methodology for membrane protein structure determination at atomic resolution by MAS NMR.
摘要：
在这里，我们使用质子检测的幻角旋转核磁共振（MASNMR）报告了脂质双层中Opa60的结构。与先前报道的去污剂结构相比，包含近天然寡糖脂质的制剂显示出稳定的跨膜β桶的一致图像，其结构化区域略有增加。已知与宿主蛋白相互作用的大可变环无法被检测到，即使在脂质双层环境中也证实了它们的动态性质。该结构为研究Opa60在淋球菌感染中的功能作用提供了起点，这被理解为涉及与宿主蛋白的相互作用。同时,它证明了通过MASNMR以原子分辨率测定膜蛋白结构的质子检测方法的最新进展。
