8JW0
PSI-AcpPCI supercomplex from Amphidinium carterae
8JW0 の概要
エントリーDOI | 10.2210/pdb8jw0/pdb |
EMDBエントリー | 36678 |
分子名称 | Photosystem I PsaA, Photosystem I PsaL, Photosystem I PsaM, ... (40 entities in total) |
機能のキーワード | photosysrem i, photosynthesis, dinoflagellate |
由来する生物種 | Amphidinium carterae 詳細 |
タンパク質・核酸の鎖数 | 29 |
化学式量合計 | 931225.15 |
構造登録者 | |
主引用文献 | Li, X.,Li, Z.,Wang, F.,Zhao, S.,Xu, C.,Mao, Z.,Duan, J.,Feng, Y.,Yang, Y.,Shen, L.,Wang, G.,Yang, Y.,Yu, L.J.,Sang, M.,Han, G.,Wang, X.,Kuang, T.,Shen, J.R.,Wang, W. Structures and organizations of PSI-AcpPCI supercomplexes from red tidal and coral symbiotic photosynthetic dinoflagellates. Proc.Natl.Acad.Sci.USA, 121:e2315476121-e2315476121, 2024 Cited by PubMed Abstract: Marine photosynthetic dinoflagellates are a group of successful phytoplankton that can form red tides in the ocean and also symbiosis with corals. These features are closely related to the photosynthetic properties of dinoflagellates. We report here three structures of photosystem I (PSI)-chlorophylls (Chls) /-peridinin protein complex (PSI-AcpPCI) from two species of dinoflagellates by single-particle cryoelectron microscopy. The crucial PsaA/B subunits of a red tidal dinoflagellate are remarkably smaller and hence losing over 20 pigment-binding sites, whereas its PsaD/F/I/J/L/M/R subunits are larger and coordinate some additional pigment sites compared to other eukaryotic photosynthetic organisms, which may compensate for the smaller PsaA/B subunits. Similar modifications are observed in a coral symbiotic dinoflagellate species, where two additional core proteins and fewer AcpPCIs are identified in the PSI-AcpPCI supercomplex. The antenna proteins AcpPCIs in dinoflagellates developed some loops and pigment sites as a result to accommodate the changed PSI core, therefore the structures of PSI-AcpPCI supercomplex of dinoflagellates reveal an unusual protein assembly pattern. A huge pigment network comprising Chls and and various carotenoids is revealed from the structural analysis, which provides the basis for our deeper understanding of the energy transfer and dissipation within the PSI-AcpPCI supercomplex, as well as the evolution of photosynthetic organisms. PubMed: 38319970DOI: 10.1073/pnas.2315476121 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.9 Å) |
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