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Publication Abstract from PubMed

Acaryochloris marina is a unique cyanobacterium using chlorophyll d (Chl d) as its major pigment and thus can use far-red light for photosynthesis. Photosystem II (PSII) of A. marina 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 A. marina 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.

Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyll d-containing cyanobacterium.,Shen L, Gao Y, Tang K, Qi R, Fu L, Chen JH, Wang W, Ma X, Li P, Chen M, Kuang T, Zhang X, Shen JR, Wang P, Han G Sci Adv. 2024 Feb 23;10(8):eadk7140. doi: 10.1126/sciadv.adk7140. Epub 2024 Feb , 23. PMID:38394197^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.