7DXH
Cryo-EM structure of PSII intermediate Psb28-PSII complex
Summary for 7DXH
Entry DOI | 10.2210/pdb7dxh/pdb |
EMDB information | 30909 |
Descriptor | Photosystem II reaction center Psb28 protein, Photosystem II reaction center protein L, Photosystem II reaction center protein M, ... (31 entities in total) |
Functional Keywords | photosystem ii; cryo-em; assembly; repair; psb28; tsl0063, plant protein |
Biological source | Thermosynechococcus vulcanus More |
Total number of polymer chains | 18 |
Total formula weight | 312886.50 |
Authors | Sui, S.F.,Shen, J.R.,Han, G.Y.,Xiao, Y.N.,Huang, G.Q. (deposition date: 2021-01-18, release date: 2021-06-30, Last modification date: 2024-06-05) |
Primary citation | Xiao, Y.,Huang, G.,You, X.,Zhu, Q.,Wang, W.,Kuang, T.,Han, G.,Sui, S.F.,Shen, J.R. Structural insights into cyanobacterial photosystem II intermediates associated with Psb28 and Tsl0063. Nat.Plants, 7:1132-1142, 2021 Cited by PubMed Abstract: Photosystem II (PSII) is a multisubunit pigment-protein complex and catalyses light-induced water oxidation, leading to the conversion of light energy into chemical energy and the release of dioxygen. We analysed the structures of two Psb28-bound PSII intermediates, Psb28-RC47 and Psb28-PSII, purified from a psbV-deletion strain of the thermophilic cyanobacterium Thermosynechococcus vulcanus, using cryo-electron microscopy. Both Psb28-RC47 and Psb28-PSII bind one Psb28, one Tsl0063 and an unknown subunit. Psb28 is located at the cytoplasmic surface of PSII and interacts with D1, D2 and CP47, whereas Tsl0063 is a transmembrane subunit and binds at the side of CP47/PsbH. Substantial structural perturbations are observed at the acceptor side, which result in conformational changes of the quinone (Q) and non-haem iron binding sites and thus may protect PSII from photodamage during assembly. These results provide a solid structural basis for understanding the assembly process of native PSII. PubMed: 34226692DOI: 10.1038/s41477-021-00961-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.14 Å) |
Structure validation
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