7YMI
PSII-Pcb Dimer of Acaryochloris Marina
Summary for 7YMI
Entry DOI | 10.2210/pdb7ymi/pdb |
EMDB information | 33929 |
Descriptor | Photosystem II protein D1 2, Photosystem II reaction center protein L, Photosystem II reaction center protein M, ... (32 entities in total) |
Functional Keywords | photosystem ii, pcb, photosynthesis |
Biological source | Acaryochloris marina MBIC11017 More |
Total number of polymer chains | 40 |
Total formula weight | 1079015.35 |
Authors | Shen, L.L.,Gao, Y.Z.,Wang, W.D.,Zhang, X.,Shen, J.R.,Wang, P.Y.,Han, G.Y. (deposition date: 2022-07-28, release date: 2023-08-16, Last modification date: 2024-09-04) |
Primary citation | Shen, L.,Gao, Y.,Tang, K.,Qi, R.,Fu, L.,Chen, J.H.,Wang, W.,Ma, X.,Li, P.,Chen, M.,Kuang, T.,Zhang, X.,Shen, J.R.,Wang, P.,Han, G. Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyll d -containing cyanobacterium. Sci Adv, 10:eadk7140-eadk7140, 2024 Cited by PubMed Abstract: is a unique cyanobacterium using chlorophyll (Chl ) as its major pigment and thus can use far-red light for photosynthesis. Photosystem II (PSII) of associates with a number of prochlorophyte Chl-binding (Pcb) proteins to act as the light-harvesting system. We report here the cryo-electron microscopic structure of a PSII-Pcb megacomplex from at a 3.6-angstrom overall resolution and a 3.3-angstrom local resolution. The megacomplex is organized as a tetramer consisting of two PSII core dimers flanked by sixteen symmetrically related Pcb proteins, with a total molecular weight of 1.9 megadaltons. The structure reveals the detailed organization of PSII core consisting of 15 known protein subunits and an unknown subunit, the assembly of 4 Pcb antennas within each PSII monomer, and possible pathways of energy transfer within the megacomplex, providing deep insights into energy transfer and dissipation mechanisms within the PSII-Pcb megacomplex involved in far-red light utilization. PubMed: 38394197DOI: 10.1126/sciadv.adk7140 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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