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DOI | 10.1073/pnas.2016328118 |
Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping | |
Higuchi A.; Shihoya W.; Konno M.; Ikuta T.; Kandori H.; Inoue K.; Nureki O. | |
发表日期 | 2021 |
ISSN | 00278424 |
卷号 | 118期号:14 |
英文摘要 | Schizorhodopsins (SzRs), a new rhodopsin family identified in Asgard archaea, are phylogenetically located at an intermediate position between type-1 microbial rhodopsins and heliorhodopsins. SzRs work as light-driven inward H+ pumps as xenorhodopsins in bacteria. Although E81 plays an essential role in inward H+ release, the H+ is not metastably trapped in such a putative H+ acceptor, unlike the other H+ pumps. It remains elusive why SzR exhibits different kinetic behaviors in H+ release. Here, we report the crystal structure of SzR AM_5_00977 at 2.1 Å resolution. The SzR structure superimposes well on that of bacteriorhodopsin rather than heliorhodopsin, suggesting that SzRs are classified with type-1 rhodopsins. The structure-based mutagenesis study demonstrated that the residues N100 and V103 around the β-ionone ring are essential for color tuning in SzRs. The cytoplasmic parts of transmembrane helices 2, 6, and 7 are shorter than those in the other microbial rhodopsins, and thus E81 is located near the cytosol and easily exposed to the solvent by light-induced structural change. We propose a model of untrapped inward H+ release; H+ is released through the water-mediated transport network from the retinal Schiff base to the cytosol by the side of E81. Moreover, most residues on the H+ transport pathway are not conserved between SzRs and xenorhodopsins, suggesting that they have entirely different inward H+ release mechanisms. © 2021 National Academy of Sciences. All rights reserved. |
英文关键词 | Proton pump; Rhodopsin; X-ray crystallography |
语种 | 英语 |
来源期刊 | Proceedings of the National Academy of Sciences of the United States of America
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文献类型 | 期刊论文 |
条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/179983 |
作者单位 | Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Bunkyo, Tokyo, 113-0033, Japan; The Institute for Solid State Physics, The University of Tokyo, Kashiwa, 277-8581, Japan; Precursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, 4-1-8 Honcho, Saitama, Kawaguchi, 332-0012, Japan; Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa, Nagoya, 466-8555, Japan; OptoBioTechnology Research Center, Nagoya Institute of Technology, Showa, Nagoya, 466-8555, Japan |
推荐引用方式 GB/T 7714 | Higuchi A.,Shihoya W.,Konno M.,et al. Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping[J],2021,118(14). |
APA | Higuchi A..,Shihoya W..,Konno M..,Ikuta T..,Kandori H..,...&Nureki O..(2021).Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping.Proceedings of the National Academy of Sciences of the United States of America,118(14). |
MLA | Higuchi A.,et al."Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping".Proceedings of the National Academy of Sciences of the United States of America 118.14(2021). |
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