Martynowski Dariusz, Grochulski Pawel, Howard Peter S
Department of Microbiology and Immunology, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK S7N 2W8, Canada.
Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):142-9. doi: 10.1107/S0907444912042710. Epub 2013 Jan 16.
Vibrio vulnificus utilizes the type II secretion system (T2SS), culminating in a megadalton outer membrane complex called the secretin, to translocate extracellular proteins from the periplasmic space across the outer membrane. In Aeromonas hydrophila, the general secretion pathway proteins ExeA and ExeB form an inner membrane complex which interacts with peptidoglycan and is required for the assembly of the secretin composed of ExeD. In V. vulnificus, these two proteins are fused into one protein, EpsAB. Here, the crystal structure of a periplasmic domain of EpsAB (amino acids 333-584) solved by SAD phasing is presented. The crystals belonged to space group C2 and diffracted to 1.55 Å resolution.
创伤弧菌利用II型分泌系统（T2SS），最终形成一种称为分泌素的兆道尔顿外膜复合物，将周质空间中的细胞外蛋白转运穿过外膜。在嗜水气单胞菌中，一般分泌途径蛋白ExeA和ExeB形成一种内膜复合物，该复合物与肽聚糖相互作用，并且是由ExeD组成的分泌素组装所必需的。在创伤弧菌中，这两种蛋白融合成一种蛋白EpsAB。本文展示了通过单波长反常散射法（SAD）解析得到的EpsAB周质结构域（氨基酸333 - 584）的晶体结构。晶体属于空间群C2，衍射分辨率达到1.55 Å。
