Molecular mechanism of the Escherichia coli maltose transporter.

Molecular mechanism of the Escherichia coli maltose transporter.
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DOI:
10.1016/j.sbi.2013.03.011
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发表时间:
2013-08
影响因子:
6.8
通讯作者:
Chen J
Chen J
中科院分区:
生物学2区
文献类型:
--
作者:
Chen J

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atp结合盒(ABC)转运蛋白是普遍存在的膜蛋白,通过脂质双分子层输入和输出多种物质。驱动ABC转运体研究的一个关键问题是ATP水解如何与底物易位耦合。本文以大肠杆菌麦芽糖转运蛋白为模型系统,了解ABC进口蛋白的分子机制。x射线晶体学被用来捕捉麦芽糖转运蛋白在多种构象中的结构。这些结构,解释在功能数据的光,讨论以解决以下问题:输运循环中构象变化的本质是什么?2. 底物如何激活atp酶活性?3. ATP水解如何使底物运输?
ATP-binding cassette (ABC) transporters are ubiquitous membrane proteins that import and export a large variety of materials across the lipid bilayer. A key question that drives ABC transporter research is how ATP hydrolysis is coupled to substrate translocation. This review uses the maltose transporter of Escherichia coli as a model system to understand the molecular mechanism of ABC importers. X-ray crystallography was used to capture the structures of the maltose transporter in multiple conformations. These structures, interpreted in the light of functional data, are discussed to address the following questions: 1. What is the nature of conformational changes in a transport cycle? 2. How does substrate activate ATPase activity? 3. How does ATP hydrolysis enable substrate transport?
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