光系统II
生物发生
化学
结晶学
生物物理学
光化学
光合作用
生物
生物化学
基因
作者
Jure Zabret,Stefan Bohn,Sandra K. Schuller,Oliver Arnolds,Madeline Möller,Jakob Meier‐Credo,Pasqual Liauw,Aaron Chan,Emad Tajkhorshid,Julian D. Langer,Raphael Stoll,Anja Krieger‐Liszkay,Benjamin D. Engel,Till Rudack,Jan M. Schuller,Marc M. Nowaczyk
出处
期刊:Nature plants
[Springer Nature]
日期:2021-04-12
卷期号:7 (4): 524-538
被引量:133
标识
DOI:10.1038/s41477-021-00895-0
摘要
Biogenesis of photosystem II (PSII), nature's water-splitting catalyst, is assisted by auxiliary proteins that form transient complexes with PSII components to facilitate stepwise assembly events. Using cryo-electron microscopy, we solved the structure of such a PSII assembly intermediate from Thermosynechococcus elongatus at 2.94 Å resolution. It contains three assembly factors (Psb27, Psb28 and Psb34) and provides detailed insights into their molecular function. Binding of Psb28 induces large conformational changes at the PSII acceptor side, which distort the binding pocket of the mobile quinone (QB) and replace the bicarbonate ligand of non-haem iron with glutamate, a structural motif found in reaction centres of non-oxygenic photosynthetic bacteria. These results reveal mechanisms that protect PSII from damage during biogenesis until water splitting is activated. Our structure further demonstrates how the PSII active site is prepared for the incorporation of the Mn4CaO5 cluster, which performs the unique water-splitting reaction.
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