9EVX
cryoEM structure of Photosystem II averaged across S2-S3 states at 1.71 Angstrom resolution
This is a non-PDB format compatible entry.
Summary for 9EVX
| Entry DOI | 10.2210/pdb9evx/pdb |
| EMDB information | 50019 |
| Descriptor | Photosystem II protein D1 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (36 entities in total) |
| Functional Keywords | photosystem ii core complex, mn cluster, water oxidation, metal binding protein |
| Biological source | Thermosynechococcus vestitus BP-1 More |
| Total number of polymer chains | 38 |
| Total formula weight | 759946.36 |
| Authors | Hussein, R.,Graca, A.,Zouni, A.,Messinger, J.,Schroder, W.P. (deposition date: 2024-04-02, release date: 2024-06-12, Last modification date: 2024-11-06) |
| Primary citation | Hussein, R.,Graca, A.,Forsman, J.,Aydin, A.O.,Hall, M.,Gaetcke, J.,Chernev, P.,Wendler, P.,Dobbek, H.,Messinger, J.,Zouni, A.,Schroder, W.P. Cryo-electron microscopy reveals hydrogen positions and water networks in photosystem II. Science, 384:1349-1355, 2024 Cited by PubMed Abstract: Photosystem II starts the photosynthetic electron transport chain that converts solar energy into chemical energy and thus sustains life on Earth. It catalyzes two chemical reactions: water oxidation to molecular oxygen and plastoquinone reduction. Coupling of electron and proton transfer is crucial for efficiency; however, the molecular basis of these processes remains speculative owing to uncertain water binding sites and the lack of experimentally determined hydrogen positions. We thus collected high-resolution cryo-electron microscopy data of fully hydrated photosystem II from the thermophilic cyanobacterium to a final resolution of 1.71 angstroms. The structure reveals several previously undetected partially occupied water binding sites and more than half of the hydrogen and proton positions. This clarifies the pathways of substrate water binding and plastoquinone B protonation. PubMed: 38900892DOI: 10.1126/science.adn6541 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.71 Å) |
Structure validation
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