气候变化领域集成服务门户(CCPortal): High-resolution structural insights into the heliorhodopsin family

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DOI	10.1073/pnas.1915888117
	High-resolution structural insights into the heliorhodopsin family
	Kovalev K.; Volkov D.; Astashkin R.; Alekseev A.; Gushchin I.; Haro-Moreno J.M.; Chizhov I.; Siletsky S.; Mamedov M.; Rogachev A.; Balandin T.; Borshchevskiy V.; Popov A.; Bourenkov G.; Bamberg E.; Rodriguez-Valera F.; Büldt G.; Gordeliy V.
发表日期	2020
ISSN	0027-8424
起始页码	4131
结束页码	4141
卷号	117 期号:8
英文摘要	Rhodopsins are the most abundant light-harvesting proteins. A new family of rhodopsins, heliorhodopsins (HeRs), has recently been discovered. Unlike in the known rhodopsins, in HeRs the N termini face the cytoplasm. The function of HeRs remains unknown. We present the structures of the bacterial HeR-48C12 in two states at the resolution of 1.5 Å, which highlight its remarkable difference from all known rhodopsins. The interior of HeR’s extracellular part is completely hydrophobic, while the cytoplasmic part comprises a cavity (Schiff base cavity [SBC]) surrounded by charged amino acids and containing a cluster of water molecules, presumably being a primary proton acceptor from the Schiff base. At acidic pH, a planar triangular molecule (acetate) is present in the SBC. Structure-based bioinformatic analysis identified 10 subfamilies of HeRs, suggesting their diverse biological functions. The structures and available data suggest an enzymatic activity of HeR-48C12 subfamily and their possible involvement in fundamental redox biological processes. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Crystal structure; Membrane protein; Retinal; Rhodopsin; X-ray crystallography
语种	英语
scopus关键词	amino acid; heliorhodopsin; membrane protein; rhodopsin; Schiff base; unclassified drug; rhodopsin; Article; bacterial strain; biological phenomena and functions concerning the entire organism; cluster analysis; cytoplasm; dimerization; enzyme activity; hydrophobicity; nonhuman; pH; priority journal; protein analysis; protein expression; protein family; protein function; protein purification; protein structure; structural bioinformatics; biology; chemistry; molecular model; photolysis; protein conformation; Computational Biology; Hydrogen-Ion Concentration; Models, Molecular; Photolysis; Protein Conformation; Rhodopsins, Microbial
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/161050
作者单位	Kovalev, K., Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-Commission for Atomic Energy (CEA)-CNRS, Grenoble, 38000, France, Institute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, Jülich, 52428, Germany, Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, 52428, Germany, Research Center for Mechanisms of Aging and Age Related Diseases, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, 141701, Russian Federation, Institute of Crystallography, University of Aachen (Rheinisch-Westfälische Technische Hochschule Aachen [RWTH]), Aachen, 52062, Germany; Volkov, D., Institute of Biological Information Processing (Institute of Biological Information Processing: Structural Biochemistry), Forschungszentrum Jülich, Jülich, 52428, Germany, Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, 52428, Germany; Astashkin, R., Inst...
推荐引用方式 GB/T 7714	Kovalev K.,Volkov D.,Astashkin R.,et al. High-resolution structural insights into the heliorhodopsin family[J],2020,117(8).
APA	Kovalev K..,Volkov D..,Astashkin R..,Alekseev A..,Gushchin I..,...&Gordeliy V..(2020).High-resolution structural insights into the heliorhodopsin family.Proceedings of the National Academy of Sciences of the United States of America,117(8).
MLA	Kovalev K.,et al."High-resolution structural insights into the heliorhodopsin family".Proceedings of the National Academy of Sciences of the United States of America 117.8(2020).