5MDX
Cryo-EM structure of the PSII supercomplex from Arabidopsis thaliana
Summary for 5MDX
Entry DOI | 10.2210/pdb5mdx/pdb |
EMDB information | 3491 |
Descriptor | Photosystem II protein D1, Photosystem II reaction center protein L, Photosystem II reaction center protein M, ... (25 entities in total) |
Functional Keywords | photosynthesis, photosystem ii supercomplex, single particle analysis |
Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
Total number of polymer chains | 50 |
Total formula weight | 1272946.91 |
Authors | van Bezouwen, L.S.,Caffarri, S.,Kale, R.S.,Kouril, R.,Thunnissen, A.M.W.H.,Oostergetel, G.T.,Boekema, E.J. (deposition date: 2016-11-13, release date: 2017-06-21, Last modification date: 2019-04-24) |
Primary citation | van Bezouwen, L.S.,Caffarri, S.,Kale, R.S.,Kouril, R.,Thunnissen, A.W.H.,Oostergetel, G.T.,Boekema, E.J. Subunit and chlorophyll organization of the plant photosystem II supercomplex. Nat Plants, 3:17080-17080, 2017 Cited by PubMed Abstract: Photosystem II (PSII) is a light-driven protein, involved in the primary reactions of photosynthesis. In plant photosynthetic membranes PSII forms large multisubunit supercomplexes, containing a dimeric core and up to four light-harvesting complexes (LHCs), which act as antenna proteins. Here we solved a three-dimensional (3D) structure of the CSM supercomplex from Arabidopsis thaliana using cryo-transmission electron microscopy (cryo-EM) and single-particle analysis at an overall resolution of 5.3 Å. Using a combination of homology modelling and restrained refinement against the cryo-EM map, it was possible to model atomic structures for all antenna complexes and almost all core subunits. We located all 35 chlorophylls of the core region based on the cyanobacterial PSII structure, whose positioning is highly conserved, as well as all the chlorophylls of the LHCII S and M trimers. A total of 13 and 9 chlorophylls were identified in CP26 and CP24, respectively. Energy flow from LHC complexes to the PSII reaction centre is proposed to follow preferential pathways: CP26 and CP29 directly transfer to the core using several routes for efficient transfer; the S trimer is directly connected to CP43 and the M trimer can efficiently transfer energy to the core through CP29 and the S trimer. PubMed: 28604725DOI: 10.1038/nplants.2017.80 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (5.3 Å) |
Structure validation
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