Structure of the maize photosystem I supercomplex with light-harvesting complexes I and II

被引:174
作者
Pan, Xiaowei [1 ]
Ma, Jun [1 ]
Su, Xiaodong [1 ]
Cao, Peng [1 ]
Chang, Wenrui [1 ,2 ]
Liu, Zhenfeng [1 ,2 ]
Zhang, Xinzheng [1 ,2 ,3 ]
Li, Mei [1 ]
机构
[1] Chinese Acad Sci, CAS Ctr Excellence Biomacromol, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[3] Chinese Acad Sci, Inst Biophys, Ctr Biol Imaging, CAS Ctr Excellence Biomacromol, Beijing 100101, Peoples R China
基金
中国国家自然科学基金; 国家重点研发计划;
关键词
A/B BINDING-PROTEINS; STATE TRANSITIONS; ELECTRON-TRANSFER; PHOTOSYNTHETIC ACCLIMATION; ARABIDOPSIS-THALIANA; THYLAKOID MEMBRANE; PSI; SUBUNIT; ANTENNA; LHCII;
D O I
10.1126/science.aat1156
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Plants regulate photosynthetic light harvesting to maintain balanced energy flux into photosystems I and II (PSI and PSII). Under light conditions favoring PSII excitation, the PSII antenna, light-harvesting complex II (LHCII), is phosphorylated and forms a supercomplex with PSI core and the PSI antenna, light-harvesting complex I (LHCI). Both LHCI and LHCII then transfer excitation energy to the PSI core. We report the structure of maize PSI-LHCI-LHCII solved by cryo electron microscopy, revealing the recognition site between LHCII and PSI. The PSI subunits PsaN and PsaO are observed at the PSI-LHCI interface and the PSI-LHCII interface, respectively. Each subunit relays excitation to PSI core through a pair of chlorophyll molecules, thus revealing previously unseen paths for energy transfer between the antennas and the PSI core.
引用
收藏
页码:1109 / 1112
页数:4
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