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Structural insights into the unusual core photocomplex from a triply extremophilic purple bacterium,Halorhodospira halochloris

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Journal of Integrative Plant Biology 2024年第10期66卷 2262-2272页

作者： Chen-Hui Qi Guang-Lei Wang Fang-Fang Wang Jie Wang Xiang-Ping Wang Mei-Juan Zou Fei Ma Michael T.Madigan Yukihiro Kimura Zheng-Yu Wang-Otomo Long-Jiang Yu Key Laboratory of Photobiology Photosynthesis Research CenterInstitute of BotanyChinese Academy of SciencesBeijing 100093China University of Chinese Academy of Sciences Beijing 100049China Zhangjiang Lab National Facility for Protein Science in ShanghaiShanghai Advanced Research InstituteChinese Academy of SciencesShanghai 201210China Department of Microbiology School of Biological SciencesSouthern Illinois UniversityCarbondaleIL 62901USA Department of Agrobioscience Graduate School of Agricultural ScienceKobe UniversityNadaKobe 657-8501Japan Faculty of Science Ibaraki UniversityMito 310-8512Japan

Halorhodospira(Hlr.)halochloris is a triply extremophilic phototrophic purple sulfur bacterium,as it is thermophilic,alkaliphilic,and extremely *** light-harvesting-reaction center(LH1–RC)core complex of this bacterium displays an LH1-Q_(y)transition at 1,016 nm,which is the lowest-energy wavelength absorption among all known *** we report the cryo-EM structure of the LH1–RC at 2.42?*** LH1 complex forms a tricyclic ring structure composed of 16αβγ-polypeptides and oneαβ-heterodimer around the *** the cryo-EM density map,two previously unrecognized integral membrane proteins,referred to as protein G and protein Q,were *** of these proteins are single transmembrane-spanning helices located between the LH1 ring and the RC Lsubunit and are absent from the LH1–RC complexes of all other purple bacteria of which the structures have been determined so *** bacteriochlorophyll b molecules(B1020)located on the periplasmic side of the *** membrane,there are also two arrays of bacteriochlorophyll b molecules(B800 and B820)located on the cytoplasmic *** a single copy of a carotenoid(lycopene)was resolved in the *** LH1–α3β3 and this was positioned within the *** potential quinone channel should be the space between the LH1–α3β3 that accommodates the single lycopene but does not contain aγ-polypeptide,B800 and *** results provide a structural explanation for the unusual Q_(y)red shift and carotenoid absorption in the *** spectrum and reveal new insights into photosynthetic mechanisms employed by a species that thrives under the harshest conditions of any phototrophic microorganism known.

关键词： cryo-EM LH1-RC single carotenoid three bacteriochlorophyll b molecules triply extremophilic purple bacterium unusual qy red shift

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