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Zabret, J.* ; Bohn, S.* ; Schuller, S.K.* ; Arnolds, O.* ; Möller, M.* ; Meier-Credo, J.* ; Liauw, P.* ; Chan, A.* ; Tajkhorshid, E.* ; Langer, J.D.* ; Stoll, R.* ; Krieger-Liszkay, A.* ; Engel, B.D. ; Rudack, T.* ; Schuller, J.M.* ; Nowaczyk, M.M.*

Structural insights into photosystem II assembly.

Nat. Plants 7, 524–538 (2021)
Open Access Green as soon as Postprint is submitted to ZB.
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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Publication type Article: Journal article
Document type Scientific Article
ISSN (print) / ISBN 2055-026X
e-ISSN 2055-0278
Journal Nature Plants
Quellenangaben Volume: 7, Issue: , Pages: 524–538 Article Number: , Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Helmholtz Pioneer Campus (HPC)
Grants Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.)
Deutsche Forschungsgemeinschaft (German Research Foundation)
Agence Nationale de la Recherche (French National Research Agency)