8ZEE
Cryo-EM structure of an intermediate-state PSII-PRF2' complex during the process of photosystem II repair
Summary for 8ZEE
| Entry DOI | 10.2210/pdb8zee/pdb |
| EMDB information | 60026 |
| Descriptor | Photosystem II CP47 reaction center protein, Photosystem II reaction center protein T, Photosystem II reaction center protein Psb30, ... (28 entities in total) |
| Functional Keywords | photosynthesis |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 16 |
| Total formula weight | 312053.74 |
| Authors | |
| Primary citation | Li, A.,You, T.,Pang, X.,Wang, Y.,Tian, L.,Li, X.,Liu, Z. Structural basis for an early stage of the photosystem II repair cycle in Chlamydomonas reinhardtii. Nat Commun, 15:5211-5211, 2024 Cited by PubMed Abstract: Photosystem II (PSII) catalyzes water oxidation and plastoquinone reduction by utilizing light energy. It is highly susceptible to photodamage under high-light conditions and the damaged PSII needs to be restored through a process known as the PSII repair cycle. The detailed molecular mechanism underlying the PSII repair process remains mostly elusive. Here, we report biochemical and structural features of a PSII-repair intermediate complex, likely arrested at an early stage of the PSII repair process in the green alga Chlamydomonas reinhardtii. The complex contains three protein factors associated with a damaged PSII core, namely Thylakoid Enriched Factor 14 (TEF14), Photosystem II Repair Factor 1 (PRF1), and Photosystem II Repair Factor 2 (PRF2). TEF14, PRF1 and PRF2 may facilitate the release of the manganese-stabilizing protein PsbO, disassembly of peripheral light-harvesting complexes from PSII and blockage of the Q site, respectively. Moreover, an α-tocopherol quinone molecule is located adjacent to the heme group of cytochrome b, potentially fulfilling a photoprotective role by preventing the generation of reactive oxygen species. PubMed: 38890314DOI: 10.1038/s41467-024-49532-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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