8W4O
Structure of PSII-FCPII-G/H complex in the PSII-FCPII supercomplex from Cyclotella meneghiniana
Summary for 8W4O
Entry DOI | 10.2210/pdb8w4o/pdb |
EMDB information | 37267 |
Descriptor | FCPII-G, Fucoxanthin chlorophyll a/c binding protein, (3S,3'R,5R,6S,7cis)-7',8'-didehydro-5,6-dihydro-5,6-epoxy-beta,beta-carotene-3,3'-diol, FCPII-H2, Fucoxanthin chlorophyll a/c binding protein, ... (10 entities in total) |
Functional Keywords | psii-fcpii, photosynthesis |
Biological source | Stephanocyclus meneghinianus More |
Total number of polymer chains | 3 |
Total formula weight | 97617.78 |
Authors | |
Primary citation | Zhao, S.,Shen, L.,Li, X.,Tao, Q.,Li, Z.,Xu, C.,Zhou, C.,Yang, Y.,Sang, M.,Han, G.,Yu, L.J.,Kuang, T.,Shen, J.R.,Wang, W. Structural insights into photosystem II supercomplex and trimeric FCP antennae of a centric diatom Cyclotella meneghiniana. Nat Commun, 14:8164-8164, 2023 Cited by PubMed Abstract: Diatoms 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. PubMed: 38071196DOI: 10.1038/s41467-023-44055-8 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.23 Å) |
Structure validation
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