Chen Yuanyuan, Capponi Sara, Zhu Lu, Gellenbeck Patrick, Freites J Alfredo, White Stephen H, Dalbey Ross E
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Department of Physiology and Biophysics, University of California, Irvine, CA 92697, USA.
Structure. 2017 Sep 5;25(9):1403-1414.e3. doi: 10.1016/j.str.2017.07.008. Epub 2017 Aug 24.
The YidC/Oxa1/Alb3 family of membrane proteins function to insert proteins into membranes in bacteria, mitochondria, and chloroplasts. Recent X-ray structures of YidC from Bacillus halodurans and Escherichia coli revealed a hydrophilic groove that is accessible from the lipid bilayer and the cytoplasm. Here, we explore the water accessibility within the conserved core region of the E. coli YidC using in vivo cysteine alkylation scanning and molecular dynamics (MD) simulations of YidC in POPE/POPG membranes. As expected from the structure, YidC possesses an aqueous membrane cavity localized to the membrane inner leaflet. Both the scanning data and the MD simulations show that the lipid-exposed transmembrane helices 3, 4, and 5 are short, leading to membrane thinning around YidC. Close examination of the MD data reveals previously unrecognized structural features that are likely important for protein stability and function.
YidC/Oxa1/Alb3膜蛋白家族的功能是将蛋白质插入细菌、线粒体和叶绿体的膜中。来自嗜碱芽孢杆菌和大肠杆菌的YidC最近的X射线结构揭示了一个可从脂质双层和细胞质进入的亲水凹槽。在这里,我们使用体内半胱氨酸烷基化扫描以及YidC在POPE/POPG膜中的分子动力学(MD)模拟,来探索大肠杆菌YidC保守核心区域内的水可及性。正如从结构中预期的那样,YidC拥有一个位于膜内小叶的水性膜腔。扫描数据和MD模拟均表明,暴露于脂质的跨膜螺旋3、4和5很短,导致YidC周围的膜变薄。对MD数据的仔细检查揭示了以前未被识别的结构特征,这些特征可能对蛋白质的稳定性和功能很重要。