Structural insights into photosystem II assembly

Zabret, Jure and Bohn, Stefan and Schuller, Sandra K. and Arnolds, Oliver and Möller, Madeline and Meier-Credo, Jakob and Liauw, Pasqual and Chan, Aaron and Tajkhorshid, Emad and Langer, Julian D. and Stoll, Raphael and Krieger-Liszkay, Anja and Engel, Benjamin D. and Rudack, Till and Schuller, Jan M. and Nowaczyk, Marc M.. (2021) Structural insights into photosystem II assembly. Nature Plants. Scientific Reports, 7 (4). pp. 524-538.

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Official URL: https://edoc.unibas.ch/89577/

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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 Mn; 4; CaO; 5; cluster, which performs the unique water-splitting reaction.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology and Biophysics (Engel)
UniBasel Contributors:Engel, Ben
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Research
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:06 Sep 2022 10:12
Deposited On:23 Aug 2022 09:00

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