• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nature >X-ray structure of a protein-conducting channel
【24h】

X-ray structure of a protein-conducting channel

机译：蛋白质传导通道的X射线结构

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

A conserved heterotrimeric membrane protein complex, the Sec61 or SecY complex, forms a protein-conducting channel, allowing polypeptides to be transferred across or integrated into membranes. We report the crystal structure of the complex from Methanococcus jannaschii at a resolution of 3.2 A. The structure suggests that one copy of the heterotrimer serves as a functional translocation channel. The α-subunit has two linked halves, transmembrane segments 1-5 and 6-10, clamped together by the γ-subunit. A cytoplasmic funnel leading into the channel is plugged by a short helix. Plug displacement can open the channel into an 'hourglass' with a ring of hydrophobic residues at its constriction. This ring may form a seal around the translocating polypeptide, hindering the permeation of other molecules. The structure also suggests mechanisms for signal-sequence recognition and for the lateral exit of transmembrane segments of nascent membrane proteins into lipid, and indicates binding sites for partners that provide the driving force for translocation.
机译：保守的异源三聚体膜蛋白复合物Sec61或SecY复合物形成一个蛋白传导通道，使多肽可以跨膜转移或整合到膜中。我们报告了复杂的晶体结构从甲烷球菌在3.2 A的分辨率。该结构表明异三聚体的一个副本充当功能性易位通道。 α亚基有两个相连的半部分，跨膜段1-5和6-10，被γ亚基夹在一起。短螺旋塞入通向通道的细胞质漏斗。塞子的移位可以将通道打开到一个“沙漏”中，该沙漏的收缩处有一圈疏水残基。该环可在易位多肽周围形成密封，阻碍其他分子的渗透。该结构还暗示了信号序列识别的机制以及新生膜蛋白的跨膜片段侧向退出脂质的机制，并指出了为转运提供驱动力的伴侣的结合位点。

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