Nature, Received 11 March 2015 Accepted 19 April 2016 Published online 18 May 2016, doi:10.1038/nature18020
Structure of spinach photosystem II–LHCII supercomplex at 3.2 angstrom resolution
Xuepeng Wei, Xiaodong Su, Peng Cao, Xiuying Liu, Wenrui Chang, Mei Li, Xinzheng Zhang & Zhenfeng Liu
Abstract
During photosynthesis, the plant photosystem II core complex receives excitation energy from the peripheral light-harvesting complex II (LHCII). The pathways along which excitation energy is transferred between them, and their assembly mechanisms, remain to be deciphered through high-resolution structural studies. Here we report the structure of a 1.1-megadalton spinach photosystem II–LHCII supercomplex solved at 3.2 angstrom resolution through single-particle cryo-electron microscopy. The structure reveals a homodimeric supramolecular system in which each monomer contains 25 protein subunits, 105 chlorophylls, 28 carotenoids and other cofactors. Three extrinsic subunits (PsbO, PsbP and PsbQ), which are essential for optimal oxygen-evolving activity of photosystem II, form a triangular crown that shields the Mn4CaO5-binding domains of CP43 and D1. One major trimeric and two minor monomeric LHCIIs associate with each core-complex monomer, and the antenna–core interactions are reinforced by three small intrinsic subunits (PsbW, PsbH and PsbZ). By analysing the closely connected interfacial chlorophylls, we have obtained detailed insights into the energy-transfer pathways between the antenna and core complexes.
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文章链接：http://www.nature.com/nature/journal/vaop/ncurrent/full/nature18020.html
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