• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >The crystal structure of the lumenal domain of Erv41p, a protein involved in transport between the endoplasmic reticulum and Golgi apparatus
【24h】

The crystal structure of the lumenal domain of Erv41p, a protein involved in transport between the endoplasmic reticulum and Golgi apparatus

机译：Erv41p腔结构域的晶体结构，该蛋白参与内质网和高尔基体之间的运输

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

Erv41p is a conserved integral membrane protein that is known to play a role in transport between the endoplasmic reticulum and Golgi apparatus, part of the early secretory pathway of eukaryotes. However, the exact function of the protein is not known, and it shares very low sequence identity with proteins of known structure or function. Here we present the structure of the full lumenal domain of Erv41p from Saccharomyces cerevisiae, determined by X-ray crystallography to a resolution of 2.0 ?. The structure reveals the protein to be composed predominantly of two large β-sheets that form a twisted β-sandwich. Comparison to structures in the Protein Data Bank shows that the Erv41p lumenal domain displays only limited similarity to β-sandwich domains of other proteins. Analysis of the surface properties of the protein identifies an extensive patch of negative electrostatic potential on the exposed surface of one of the β-sheets, which likely forms a binding site for a ligand or interaction partner. A predominantly hydrophobic region close to the membrane interface is identified as a likely site for protein-protein interaction. This structure, the first of Erv41p or any of its homologues, provides a new starting point for studies of the roles of Erv41p and its interaction partners in the eukaryotic secretory pathway.
机译：Erv41p是一种保守的整合膜蛋白，已知在内质网和高尔基体（真核生物早期分泌途径的一部分）之间的运输中起作用。但是，该蛋白的确切功能尚不清楚，并且与已知结构或功能的蛋白具有非常低的序列同一性。在这里，我们介绍了来自酿酒酵母的Erv41p的完整腔结构域的结构，通过X射线晶体学测定到分辨率为2.0？。该结构揭示了该蛋白质主要由形成扭曲的β三明治的两个大β折叠组成。与蛋白质数据库中结构的比较表明，Erv41p管腔结构域与其他蛋白质的β夹心结构域仅表现出有限的相似性。对该蛋白质的表面特性进行分析，可以在其中一个β-折叠的暴露表面上发现大量的负静电电位，这很可能形成配体或相互作用伴侣的结合位点。靠近膜界面的主要疏水区域被确定为蛋白质与蛋白质相互作用的可能位点。这种结构是Erv41p或其任何同源物的第一个，为研究Erv41p及其相互作用伙伴在真核分泌途径中的作用提供了新的起点。

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