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The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis
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SYSNO ASEP 0575001 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis Tvůrce(i) Zhao, Z. (GB)
Vercellino, I. (AT)
Knoppová, Jana (MBU-M) RID
Sobotka, Roman (MBU-M) RID, ORCID
Murray, James W. (GB)
Nixon, Peter J. (GB)
Sazanov, Leonid A. (AT)
Komenda, Josef (MBU-M) RID, ORCIDČíslo článku 4681 Zdroj.dok. Nature Communications. - : Nature Publishing Group
Roč. 14, č. 1 (2023)Poč.str. 11 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova sp. pcc 6803 ; crystal-structure ; water-oxidation ; initial steps ; cryo-em ; protein ; complex ; d1i ; insights ; subunit Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP GX19-29225X GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 001042606700004 EID SCOPUS 85166598094 DOI 10.1038/s41467-023-40388-6 Anotace Robust oxygenic photosynthesis requires a suite of accessory factors to ensure efficient assembly and repair of the oxygen-evolving photosystem two (PSII) complex. The highly conserved Ycf48 assembly factor binds to the newly synthesized D1 reaction center polypeptide and promotes the initial steps of PSII assembly, but its binding site is unclear. Here we use cryo-electron microscopy to determine the structure of a cyanobacterial PSII D1/D2 reaction center assembly complex with Ycf48 attached. Ycf48, a 7-bladed beta propeller, binds to the amino-acid residues of D1 that ultimately ligate the water-oxidising Mn4CaO5 cluster, thereby preventing the premature binding of Mn2+ and Ca2+ ions and protecting the site from damage. Interactions with D2 help explain how Ycf48 promotes assembly of the D1/D2 complex. Overall, our work provides valuable insights into the early stages of PSII assembly and the structural changes that create the binding site for the Mn4CaO5 cluster. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2024 Elektronická adresa https://www.nature.com/articles/s41467-023-40388-6
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