海链藻
光合作用
光系统II
单体
生物物理学
光系统I
硅藻
化学
电子转移
结晶学
生物
植物
光化学
生物化学
聚合物
浮游植物
有机化学
营养物
作者
Yue Feng,Zhenhua Li,X. D. Li,Lili Shen,Xueyang Liu,Cuicui Zhou,Jin-yang Zhang,Miao Sang,Guangye Han,Wenqiang Yang,Tingyun Kuang,Wenda Wang,Jian‐Ren Shen
出处
期刊:Science Advances
[American Association for the Advancement of Science (AAAS)]
日期:2023-10-27
卷期号:9 (43)
被引量:2
标识
DOI:10.1126/sciadv.adi8446
摘要
Diatoms rely on fucoxanthin chlorophyll a/c-binding proteins (FCPs) for their great success in oceans, which have a great diversity in their pigment, protein compositions, and subunit organizations. We report a unique structure of photosystem II (PSII)-FCPII supercomplex from Thalassiosira pseudonana at 2.68-Å resolution by cryo-electron microscopy. FCPIIs within this PSII-FCPII supercomplex exist in dimers and monomers, and a homodimer and a heterodimer were found to bind to a PSII core. The FCPII homodimer is formed by Lhcf7 and associates with PSII through an Lhcx family antenna Lhcx6_1, whereas the heterodimer is formed by Lhcf6 and Lhcf11 and connects to the core together with an Lhcf5 monomer through Lhca2 monomer. An extended pigment network consisting of diatoxanthins, diadinoxanthins, fucoxanthins, and chlorophylls a/c is revealed, which functions in efficient light harvesting, energy transfer, and dissipation. These results provide a structural basis for revealing the energy transfer and dissipation mechanisms and also for the structural diversity of FCP antennas in diatoms.
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