6jlu
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/B6ZHF4_9STRA B6ZHF4_9STRA]] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.[HAMAP-Rule:MF_01378] [[http://www.uniprot.org/uniprot/B6ZHF2_9STRA B6ZHF2_9STRA]] Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.[HAMAP-Rule:MF_01386] [[http://www.uniprot.org/uniprot/B7XBY7_9STRA B7XBY7_9STRA]] One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.[HAMAP-Rule:MF_00752] | [[http://www.uniprot.org/uniprot/B6ZHF4_9STRA B6ZHF4_9STRA]] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.[HAMAP-Rule:MF_01378] [[http://www.uniprot.org/uniprot/B6ZHF2_9STRA B6ZHF2_9STRA]] Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.[HAMAP-Rule:MF_01386] [[http://www.uniprot.org/uniprot/B7XBY7_9STRA B7XBY7_9STRA]] One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.[HAMAP-Rule:MF_00752] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Diatoms play important roles in global primary productivity and biogeochemical cycling of carbon, in part owing to the ability of their photosynthetic apparatus to adapt to rapidly changing light intensity. We report a cryo-electron microscopy structure of the photosystem II (PSII)-fucoxanthin (Fx) chlorophyll (Chl) a/c binding protein (FCPII) supercomplex from the centric diatom Chaetoceros gracilis The supercomplex comprises two protomers, each with two tetrameric and three monomeric FCPIIs around a PSII core that contains five extrinsic oxygen-evolving proteins at the lumenal surface. The structure reveals the arrangement of a huge pigment network that contributes to efficient light energy harvesting, transfer, and dissipation processes in the diatoms. | ||
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| + | The pigment-protein network of a diatom photosystem II-light-harvesting antenna supercomplex.,Pi X, Zhao S, Wang W, Liu D, Xu C, Han G, Kuang T, Sui SF, Shen JR Science. 2019 Aug 2;365(6452). pii: 365/6452/eaax4406. doi:, 10.1126/science.aax4406. PMID:31371578<ref>PMID:31371578</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6jlu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 17:23, 14 August 2019
Structure of PSII-FCP supercomplex from a centric diatom Chaetoceros gracilis at 3.02 angstrom resolution
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