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Cryo-EM structures of light-harvesting 2 complexes from Rhodopseudomonas palustris reveal the molecular origin of absorption tuning
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SYSNO ASEP 0565507 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Cryo-EM structures of light-harvesting 2 complexes from Rhodopseudomonas palustris reveal the molecular origin of absorption tuning Tvůrce(i) Qian, P. (NL)
Nguyen-Phan, C. T. (GB)
Gardiner, Alastair T. (MBU-M) ORCID
Croll, T. I. (GB)
Roszak, A. W. (GB)
Southall, J. (GB)
Jackson, P. J. (GB)
Vasilev, C. (GB)
Castro-Hartmann, P. (NL)
Sader, K. (NL)
Hunter, C. N. (GB)
Cogdell, R. J. (GB)Číslo článku e2210109119 Zdroj.dok. Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences - ISSN 0027-8424
Roč. 119, č. 43 (2022)Poč.str. 11 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova absorption band turning ; cryo-EM ; light-harvesting complex ; photosynthesis ; Rhodopseudomonas palustris Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 001016355500006 EID SCOPUS 85140271581 DOI https://doi.org/10.1073/pnas.2210109119 Anotace The genomes of some purple photosynthetic bacteria contain a multigene puc family encoding a series of α- and β-polypeptides that together form a heterogeneous antenna of light-harvesting 2 (LH2) complexes. To unravel this complexity, we generated four sets of puc deletion mutants in Rhodopseudomonas palustris, each encoding a single type of pucBA gene pair and enabling the purification of complexes designated as PucA-LH2, PucB-LH2, PucD-LH2, and PucE-LH2. The structures of all four purified LH2 complexes were determined by cryogenic electron microscopy (cryo-EM) at resolutions ranging from 2.7 to 3.6 Å. Uniquely, each of these complexes contains a hitherto unknown polypeptide, γ, that forms an extended undulating ribbon that lies in the plane of the membrane and that encloses six of the nine LH2 αβ-subunits. The γ-subunit, which is located near to the cytoplasmic side of the complex, breaks the C9 symmetry of the LH2 complex and binds six extra bacteriochlorophylls (BChls) that enhance the 800-nm absorption of each complex. The structures show that all four complexes have two complete rings of BChls, conferring absorption bands centered at 800 and 850 nm on the PucA-LH2, PucB-LH2, and PucE-LH2 complexes, but, unusually, the PucD-LH2 antenna has only a single strong near-infared (NIR) absorption peak at 803 nm. Comparison of the cryo-EM structures of these LH2 complexes reveals altered patterns of hydrogen bonds between LH2 αβ-side chains and the bacteriochlorin rings, further emphasizing the major role that H bonds play in spectral tuning of bacterial antenna complexes. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2023 Elektronická adresa https://www.pnas.org/doi/10.1073/pnas.2210109119
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