Summary for 7PNK
| Entry DOI | 10.2210/pdb7pnk/pdb |
| EMDB information | 13548 |
| Descriptor | Photosystem II protein D1, Photosystem II reaction center protein J, Photosystem II reaction center protein K, ... (51 entities in total) |
| Functional Keywords | green algae, photosystem ii, thylakoid, oxygen evolving complex, cryo-em, stacking, photosynthesis |
| Biological source | Dunaliella salina More |
| Total number of polymer chains | 44 |
| Total formula weight | 865683.01 |
| Authors | Caspy, I.,Fadeeva, M.,Mazor, Y.,Nelson, N. (deposition date: 2021-09-07, release date: 2022-08-17, Last modification date: 2024-11-13) |
| Primary citation | Caspy, I.,Fadeeva, M.,Mazor, Y.,Nelson, N. Structure of Dunaliella Photosystem II reveals conformational flexibility of stacked and unstacked supercomplexes. Elife, 12:-, 2023 Cited by PubMed Abstract: Photosystem II (PSII) generates an oxidant whose redox potential is high enough to enable water oxidation , a substrate so abundant that it assures a practically unlimited electron source for life on earth . Our knowledge on the mechanism of water photooxidation was greatly advanced by high-resolution structures of prokaryotic PSII . Here, we show high-resolution cryogenic electron microscopy (cryo-EM) structures of eukaryotic PSII from the green alga at two distinct conformations. The conformers are also present in stacked PSII, exhibiting flexibility that may be relevant to the grana formation in chloroplasts of the green lineage. CP29, one of PSII associated light-harvesting antennae, plays a major role in distinguishing the two conformations of the supercomplex. We also show that the stacked PSII dimer, a form suggested to support the organisation of thylakoid membranes , can appear in many different orientations providing a flexible stacking mechanism for the arrangement of grana stacks in thylakoids. Our findings provide a structural basis for the heterogenous nature of the eukaryotic PSII on multiple levels. PubMed: 36799903DOI: 10.7554/eLife.81150 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.61 Å) |
Structure validation
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