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Structural insights into photosystem II assembly

MPS-Authors
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Bohn,  Stefan
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Schuller,  Sandra K.
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;
CryoEM of Molecular Machines, SYNMIKRO Research Center and Department of Chemistry, Philipps University of Marburg, Marburg, Germany;

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Meier-Credo,  Jakob       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David       
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;
Proteomics (Scientific Service Group), Max Planck Institute for Brain Research, Max Planck Society;

Engel,  Benjamin D.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;
Helmholtz Pioneer Campus, Helmholtz Zentrum München, Neuherberg, Germany;
Department of Chemistry, Technical University of Munich, Garching, Germany;

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Schuller,  Jan Michael
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Zabret, J., Bohn, S., Schuller, S. K., Arnolds, O., Möller, M., Meier-Credo, J., et al. (2021). Structural insights into photosystem II assembly. Nature Plants, 7, 524-538. doi:10.1038/s41477-021-00895-0.


Cite as: https://hdl.handle.net/21.11116/0000-0008-500B-2
Abstract
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.