8BD3
Cryo-EM structure of the Photosystem II - LHCII supercomplex from Chlorella ohadi
This is a non-PDB format compatible entry.
Summary for 8BD3
| Entry DOI | 10.2210/pdb8bd3/pdb |
| EMDB information | 15973 |
| Descriptor | Chlorophyll a-b binding protein, chloroplastic, Cytochrome b559 subunit beta, Photosystem II reaction center protein H, ... (49 entities in total) |
| Functional Keywords | green alga, psii, c.ohadi, membrane protein, cryo-em, photosynthesis |
| Biological source | Chlorella ohadii More |
| Total number of polymer chains | 66 |
| Total formula weight | 1723567.67 |
| Authors | Fadeeva, M.,Klaiman, D.,Caspy, I.,Nelson, N. (deposition date: 2022-10-18, release date: 2023-08-09, Last modification date: 2023-08-23) |
| Primary citation | Fadeeva, M.,Klaiman, D.,Caspy, I.,Nelson, N. Structure of Chlorella ohadii Photosystem II Reveals Protective Mechanisms against Environmental Stress. Cells, 12:-, 2023 Cited by PubMed Abstract: Green alga is known for its ability to carry out photosynthesis under harsh conditions. Using cryogenic electron microscopy (cryoEM), we obtained a high-resolution structure of PSII at 2.72 Å. This structure revealed 64 subunits, which encompassed 386 chlorophylls, 86 carotenoids, four plastoquinones, and several structural lipids. At the luminal side of PSII, a unique subunit arrangement was observed to protect the oxygen-evolving complex. This arrangement involved PsbO (OEE1), PsbP (OEE2), PsbB, and PsbU (a homolog of plant OEE3). PsbU interacted with PsbO, PsbC, and PsbP, thereby stabilizing the shield of the oxygen-evolving complex. Significant changes were also observed at the stromal electron acceptor side. PsbY, identified as a transmembrane helix, was situated alongside PsbF and PsbE, which enclosed cytochrome . Supported by the adjacent C-terminal helix of Psb10, these four transmembrane helices formed a bundle that shielded cytochrome from the surrounding solvent. Moreover, the bulk of Psb10 formed a protective cap, which safeguarded the quinone site and likely contributed to the stacking of PSII complexes. Based on our findings, we propose a protective mechanism that prevents Q (plastoquinone B) from becoming fully reduced. This mechanism offers insights into the regulation of electron transfer within PSII. PubMed: 37566050DOI: 10.3390/cells12151971 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.73 Å) |
Structure validation
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