Department of Systems Biology and Division of Life Sciences, Yonsei University, 50 Yonsei-ro, Seoul 03722, Republic of Korea.
Department of Biochemistry and Division of Life Sciences, Yonsei University, 50 Yonsei-ro, Seoul 03722, Republic of Korea.
Nat Commun. 2016 Aug 24;7:12677. doi: 10.1038/ncomms12677.
A novel light-driven chloride-pumping rhodopsin (ClR) containing an 'NTQ motif' in its putative ion conduction pathway has been discovered and functionally characterized in a genomic analysis study of a marine bacterium. Here we report the crystal structure of ClR from the flavobacterium Nonlabens marinus S1-08(T) determined under two conditions at 2.0 and 1.56 Å resolutions. The structures reveal two chloride-binding sites, one around the protonated Schiff base and the other on a cytoplasmic loop. We identify a '3 omega motif' formed by three non-consecutive aromatic amino acids that is correlated with the B-C loop orientation. Detailed ClR structural analyses with functional studies in E. coli reveal the chloride ion transduction pathway. Our results help understand the molecular mechanism and physiological role of ClR and provide a structural basis for optogenetic applications.
在对海洋细菌的基因组分析研究中，发现了一种新型的光驱动氯离子泵视紫红质（ClR），其在假定的离子传导途径中含有“NTQ 基序”。在这里，我们报告了来自黄色杆菌 Nonlabens marinus S1-08（T）的 ClR 的晶体结构，该结构是在 2.0 和 1.56Å分辨率下的两种条件下确定的。这些结构揭示了两个氯离子结合位点，一个位于质子化的 Schiff 碱周围，另一个位于细胞质环上。我们确定了一个由三个非连续的芳香族氨基酸组成的“3ω基序”，该基序与 B-C 环的取向相关。通过在大肠杆菌中的功能研究对 ClR 进行详细的结构分析，揭示了氯离子转导途径。我们的研究结果有助于理解 ClR 的分子机制和生理作用，并为光遗传学应用提供了结构基础。
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