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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Structure of a periplasmic domain of the EpsAB fusion protein of the Vibrio vulnificus type II secretion system
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Structure of a periplasmic domain of the EpsAB fusion protein of the Vibrio vulnificus type II secretion system

机译:EpsAB周质的结构域创伤弧菌II型的融合蛋白分泌系统

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摘要

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? resolution.
机译:创伤弧菌利用II型分泌系统(T2SS),最终megadalton外膜复杂的称为分泌素,把从细胞外蛋白质外膜细胞周质间隙。气单胞菌属hydrophila,分泌通路ExeA和ExeB形成一个内部的蛋白质膜与复杂肽聚糖和需要组装的分泌素由交货。这两个蛋白融合成一个蛋白质,EpsAB。周质的领域EpsAB氨基酸(333 - 584)由悲伤逐步解决。属于空间群C2和衍射1.55 ?

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