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Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution
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Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution
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Journal Article
Structure of spinach photosystem II–LHCII supercomplex at 3.2 Å resolution
2016
Overview
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 Å 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 Mn
4
CaO
5
-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.
A high-resolution structural study sheds light on processes of energy transfer within the photosynthetic water-splitting machinery of plants.
Energy transfer in the photosynthetic complex
The conversion of light into usable energy within a photosynthesizing cell occurs within the light-harvesting complex (LHC) and photosystem (PS) complex. To understand this process, it is critical to know how excitation energy is transferred from the peripheral LHC antenna to the core PS structure. Zhenfeng Liu and colleagues have determined a high-resolution structure of a 1.1-MDa plant PSII–LHCII supercomplex by single-particle cryo-electron microscopy. They find that each monomer of the homodimeric supercomplex contains 25 proteins and 133 pigment cofactors. Some differences are seen compared to cyanobacterial PSII structures, but, most importantly, the ability to examine the PSII–LHCII interface permits solid predictions regarding the excitation-energy-transfer pathway.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/83
/ Humanities and Social Sciences
/ Light
/ Light-Harvesting Protein Complexes - chemistry
/ Light-Harvesting Protein Complexes - ultrastructure
/ Photosystem II Protein Complex - chemistry
/ Photosystem II Protein Complex - ultrastructure
/ Protein Subunits - chemistry
/ Proteins
/ Science
/ Spinach
