• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Structure of the minor pseudopilin EpsH from the type 2 secretion system of Vibrio cholerae
【24h】

Structure of the minor pseudopilin EpsH from the type 2 secretion system of Vibrio cholerae

机译：霍乱弧菌2型分泌系统的次要假菌素EpsH的结构

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Many Gram-negative bacteria use the multi-protein type 11 secretion system (T2SS) to selectively translocate virulence factors from the periplasmic space into the extracellular environment. In Vibrio cholerae the T2SS is called the extracellular protein secretion (Eps) system,which translocates cholera toxin and several enzymes in their folded state across the outer membrane. Five proteins of the T2SS, the pseudopilins, are thought to assemble into a pseudopilus, which may control the outer membrane pore EpsD, and participate in the active export of proteins in a "piston-like" manner. We report here the 2.0 angstrom resolution crystal structure of an N-terminally truncated variant of EpsH, a minor pseudopilin from Vibrio cholerae. While EpsH maintains an N-terminal alpha-helix and C-terminal beta-sheet consistent with the type 4a pilin fold, structural comparisons reveal major differences between the minor pseudopilin EpsH and the major pseudopilin GspG from Klebsiella oxytoca: EpsH contains a large beta-sheet in the variable domain, where GspG contains an ut-helix. Most importantly, EpsH contains at its surface a hydrophobic crevice between its variable and conserved beta-sheets, wherein a majority of the conserved residues within the EpsH family are clustered. In a tentative model of a T2SS pseudopilus with EpsH at its tip, the conserved crevice faces away from the helix axis. This conserved surface region may be critical for interacting with other proteins from the T2SS machinery. (c) 2007 Elsevier Ltd. All rights reserved.
机译：许多革兰氏阴性细菌使用11型多蛋白分泌系统（T2SS）将毒力因子从周质空间选择性转移到细胞外环境。在霍乱弧菌中，T2SS称为细胞外蛋白分泌（Eps）系统，该系统将霍乱毒素和几种酶以折叠状态转运到外膜上。 T2SS的五种蛋白质，即假菌毛蛋白，被认为组装成假菌毛，可以控制外膜孔EpsD，并以“活塞样”方式参与蛋白质的主动输出。我们在这里报告了EpsH（来自霍乱弧菌的次要假菌素）的N端截短变体的2.0埃分辨率晶体结构。虽然EpsH维持N端α-螺旋和C端β-折叠与4a型菌毛折叠一致，但结构比较显示，小假菌素EpsH和产于产酸克雷伯菌的主要假菌素GspG之间存在主要差异：可变域中的表格，其中GspG包含ut-螺旋。最重要的是，EpsH在其表面上具有可变和保守的β-折叠之间的疏水缝隙，其中EpsH家族中的大多数保守残基都聚集在一起。在以EpsH为尖端的T2SS假菌毛的暂定模型中，保守的缝隙背对螺旋轴。这个保守的表面区域对于与T2SS机械中的其他蛋白质相互作用可能至关重要。 （c）2007 Elsevier Ltd.保留所有权利。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号