Summary for 3WU2
Entry DOI | 10.2210/pdb3wu2/pdb |
Descriptor | Photosystem Q(B) protein, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (41 entities in total) |
Functional Keywords | psii, electron transport, photosynthesis, photosystem, membrane complex, transmembrane alpha-helix, oxygen evolving, water splitting, iron binding, calcium binding, manganese binding, chloride binding, formylation, hydroxylation, thylakoid membrane |
Biological source | Thermosynechococcus vulcanus More |
Total number of polymer chains | 38 |
Total formula weight | 725270.17 |
Authors | Umena, Y.,Kawakami, K.,Shen, J.R.,Kamiya, N. (deposition date: 2014-04-21, release date: 2014-09-03, Last modification date: 2020-07-29) |
Primary citation | Umena, Y.,Kawakami, K.,Shen, J.-R.,Kamiya, N. Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A Nature, 473:55-60, 2011 Cited by PubMed Abstract: Photosystem II is the site of photosynthetic water oxidation and contains 20 subunits with a total molecular mass of 350 kDa. The structure of photosystem II has been reported at resolutions from 3.8 to 2.9 Å. These resolutions have provided much information on the arrangement of protein subunits and cofactors but are insufficient to reveal the detailed structure of the catalytic centre of water splitting. Here we report the crystal structure of photosystem II at a resolution of 1.9 Å. From our electron density map, we located all of the metal atoms of the Mn(4)CaO(5) cluster, together with all of their ligands. We found that five oxygen atoms served as oxo bridges linking the five metal atoms, and that four water molecules were bound to the Mn(4)CaO(5) cluster; some of them may therefore serve as substrates for dioxygen formation. We identified more than 1,300 water molecules in each photosystem II monomer. Some of them formed extensive hydrogen-bonding networks that may serve as channels for protons, water or oxygen molecules. The determination of the high-resolution structure of photosystem II will allow us to analyse and understand its functions in great detail. PubMed: 21499260DOI: 10.1038/nature09913 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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