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Subunit and chlorophyll organization of the plant photosystem II supercomplex.

Autoři: van Bezouwen L.S., Caffarri S., Kale R.S., Kouřil R., Thunnissen A.-M.W.H., Oostergetel G.T., Boekema E.J.Publikováno : Nature Plants 3, 17080Rok: 2017

Photosystem II (PSII) is a light driven protein, which is involved in the primary reactions of photosynthesis. In plant photosynthetic membranes it commonly forms a large multi-subunit supercomplex, containing a dimeric core and up to four light harvesting complexes (LHCII) as antenna proteins. In this study we solved a high resolution 3D structure of the C2S2M2 supercomplex from Arabidopsis, using cryo-electron microscopy and single particle analysis. Overall the cryo-EM structure is solved at a resolution of 5.4 Å, however locally at the core the resolution is close to 4 Å. Using a combination of homology modelling and restrained refinement against the cryo-EM map it was possible to model atomic structures for almost all core subunits and all antenna complexes. We managed to locate all expected 35 chlorophylls of the core region based on the cyanobacterial PSII structure, which turns out to have highly conserved positions, 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. It appears that energy transfer can 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 via CP29 and the S-trimer.

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