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7NHQ

Structure of PSII-I prime (PSII with Psb28, and Psb34)

Summary for 7NHQ
Entry DOI10.2210/pdb7nhq/pdb
EMDB information12337
DescriptorPhotosystem II protein D1 1, Photosystem II reaction center protein L, Photosystem II reaction center protein M, ... (27 entities in total)
Functional Keywordsmembrane protein biogenesis assembly factors photosystem ii, photosynthesis
Biological sourceThermosynechococcus elongatus BP-1
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Total number of polymer chains17
Total formula weight311088.15
Authors
Zabret, J.,Bohn, S.,Schuller, S.K.,Arnolds, O.,Chan, A.,Tajkhorshid, E.,Stoll, R.,Engel, B.D.,Rudack, T.,Schuller, J.M.,Nowaczyk, M.M. (deposition date: 2021-02-11, release date: 2021-05-05, Last modification date: 2024-05-01)
Primary citationZabret, J.,Bohn, S.,Schuller, S.K.,Arnolds, O.,Moller, 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
Cited by
PubMed 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 (Q) 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 MnCaO cluster, which performs the unique water-splitting reaction.
PubMed: 33846594
DOI: 10.1038/s41477-021-00895-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.68 Å)
Structure validation

226707

数据于2024-10-30公开中

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