4.6 Article

Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer

期刊

出版社

ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2013.03.008

关键词

Membrane protein; Signal transduction; Retinal protein; X-ray crystallography; Protein crystallization

资金

  1. ANR France
  2. Federal Target Program Scientific and academic research cadres of innovative Russia
  3. ONEXIM, Russia

向作者/读者索取更多资源

The complex of sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII) mediates negative phototaxis in halobacteria Natronomonas pharaonis. Upon light activation NpSRII triggers, by means of NpHtrII, a signal transduction chain homologous to the two component system in eubacterial chemotaxis. Here we report on the crystal structure of the ground state of the mutant NpSRII-D75N/NpHtrIl complex in the space group I2(1)2(1)2(1). Mutations of this aspartic acid in light-driven proton pumps dramatically modify or/and inhibit protein functions. However, in vivo studies show that the similar D75N mutation retains functionality of the NpSRII/NpHtrIl complex. The structure provides the molecular basis for the explanation of the unexpected observation that the wild and the mutant complexes display identical physiological response on light excitation. (C) 2013 Elsevier B.V. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据