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登録情報 | データベース: PDB / ID: 6k33 | ||||||
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タイトル | Structure of PSI-isiA supercomplex from Thermosynechococcus vulcanus | ||||||
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![]() | PHOTOSYNTHESIS / Electron Transport | ||||||
機能・相同性 | ![]() : / photosystem I reaction center / photosystem I / photosystem I / plasma membrane-derived thylakoid membrane / chlorophyll binding / photosynthetic electron transport in photosystem I / photosynthesis / 4 iron, 4 sulfur cluster binding / membrane => GO:0016020 ...: / photosystem I reaction center / photosystem I / photosystem I / plasma membrane-derived thylakoid membrane / chlorophyll binding / photosynthetic electron transport in photosystem I / photosynthesis / 4 iron, 4 sulfur cluster binding / membrane => GO:0016020 / electron transfer activity / magnesium ion binding / metal ion binding 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.74 Å | ||||||
![]() | Akita, F. / Nagao, R. / Kato, K. / Shen, J.R. / Miyazaki, N. | ||||||
![]() | ![]() タイトル: Structure of a cyanobacterial photosystem I surrounded by octadecameric IsiA antenna proteins. 著者: Fusamichi Akita / Ryo Nagao / Koji Kato / Yoshiki Nakajima / Makio Yokono / Yoshifumi Ueno / Takehiro Suzuki / Naoshi Dohmae / Jian-Ren Shen / Seiji Akimoto / Naoyuki Miyazaki / ![]() 要旨: Iron-stress induced protein A (IsiA) is a chlorophyll-binding membrane-spanning protein in photosynthetic prokaryote cyanobacteria, and is associated with photosystem I (PSI) trimer cores, but its ...Iron-stress induced protein A (IsiA) is a chlorophyll-binding membrane-spanning protein in photosynthetic prokaryote cyanobacteria, and is associated with photosystem I (PSI) trimer cores, but its structural and functional significance in light harvesting remains unclear. Here we report a 2.7-Å resolution cryo-electron microscopic structure of a supercomplex between PSI core trimer and IsiA from a thermophilic cyanobacterium Thermosynechococcus vulcanus. The structure showed that 18 IsiA subunits form a closed ring surrounding a PSI trimer core. Detailed arrangement of pigments within the supercomplex, as well as molecular interactions between PSI and IsiA and among IsiAs, were resolved. Time-resolved fluorescence spectra of the PSI-IsiA supercomplex showed clear excitation-energy transfer from IsiA to PSI, strongly indicating that IsiA functions as an energy donor, but not an energy quencher, in the supercomplex. These structural and spectroscopic findings provide important insights into the excitation-energy-transfer and subunit assembly mechanisms in the PSI-IsiA supercomplex. | ||||||
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