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7YMI

PSII-Pcb Dimer of Acaryochloris Marina

Summary for 7YMI
Entry DOI10.2210/pdb7ymi/pdb
EMDB information33929
DescriptorPhotosystem II protein D1 2, Photosystem II reaction center protein L, Photosystem II reaction center protein M, ... (32 entities in total)
Functional Keywordsphotosystem ii, pcb, photosynthesis
Biological sourceAcaryochloris marina MBIC11017
More
Total number of polymer chains40
Total formula weight1079015.35
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 citationShen, 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: 38394197
DOI: 10.1126/sciadv.adk7140
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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