8w4p
From Proteopedia
Structure of PSII-FCPII-I/J/K complex in the PSII-FCPII supercomplex from Cyclotella meneghiniana
Structural highlights
Publication Abstract from PubMedDiatoms are dominant marine algae and contribute around a quarter of global primary productivity, the success of which is largely attributed to their photosynthetic capacity aided by specific fucoxanthin chlorophyll-binding proteins (FCPs) to enhance the blue-green light absorption under water. We purified a photosystem II (PSII)-FCPII supercomplex and a trimeric FCP from Cyclotella meneghiniana (Cm) and solved their structures by cryo-electron microscopy (cryo-EM). The structures reveal detailed organizations of monomeric, dimeric and trimeric FCP antennae, as well as distinct assemblies of Lhcx6_1 and dimeric FCPII-H in PSII core. Each Cm-PSII-FCPII monomer contains an Lhcx6_1, an FCP heterodimer and other three FCP monomers, which form an efficient pigment network for harvesting energy. More diadinoxanthins and diatoxanthins are found in FCPs, which may function to quench excess energy. The trimeric FCP contains more chlorophylls c and fucoxanthins. These diversified FCPs and PSII-FCPII provide a structural basis for efficient light energy harvesting, transfer, and dissipation in C. meneghiniana. Structural insights into photosystem II supercomplex and trimeric FCP antennae of a centric diatom Cyclotella meneghiniana.,Zhao S, Shen L, Li X, Tao Q, Li Z, Xu C, Zhou C, Yang Y, Sang M, Han G, Yu LJ, Kuang T, Shen JR, Wang W Nat Commun. 2023 Dec 9;14(1):8164. doi: 10.1038/s41467-023-44055-8. PMID:38071196[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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