- EMDB-30656: Structure of RC-LH1-PufX from Rhodobacter veldkampii -
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基本情報
登録情報
データベース: EMDB / ID: EMD-30656
タイトル
Structure of RC-LH1-PufX from Rhodobacter veldkampii
マップデータ
試料
複合体: Photosynthetic core complex featuring reaction center, LH1 and PufX
タンパク質・ペプチド: x 4種
タンパク質・ペプチド: x 2種
リガンド: x 6種
キーワード
membrane protein / light-harvesting / reaction center / pufx / PHOTOSYNTHESIS
機能・相同性
機能・相同性情報
organelle inner membrane / : / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / photosynthetic electron transport in photosystem II / membrane => GO:0016020 / metal ion binding / plasma membrane 類似検索 - 分子機能
Intrinsic membrane protein family, PufX / Intrinsic membrane protein PufX / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex ...Intrinsic membrane protein family, PufX / Intrinsic membrane protein PufX / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Light-harvesting protein B beta chain / Antenna complex, alpha/beta subunit / Light-harvesting complex / Antenna complex alpha/beta subunit / Photosynthetic reaction centre, H subunit / Bacterial photosynthetic reaction centre, H-chain, C-terminal / Photosynthetic reaction centre, M subunit / Photosynthetic reaction centre, H subunit, N-terminal / Photosynthetic reaction centre, H subunit, N-terminal domain superfamily / Photosynthetic reaction centre, H-chain N-terminal region / PRC-barrel domain / PRC-barrel domain / Photosynthetic reaction centre, L subunit / PRC-barrel-like superfamily / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. 類似検索 - ドメイン・相同性
Antenna pigment protein beta chain / Reaction center protein M chain / Uncharacterized protein / Photosynthetic reaction center subunit H / Antenna pigment protein alpha chain / Photosynthetic reaction center L subunit 類似検索 - 構成要素
Biotechnology and Biological Sciences Research Council (BBSRC)
R003890
英国
Japan Agency for Medical Research and Development (AMED)
JP20am0101082
日本
Japan Agency for Medical Research and Development (AMED)
JP20am0101115
日本
Japan Society for the Promotion of Science (JSPS)
JP 19H03162
日本
引用
ジャーナル: Sci Adv / 年: 2021 タイトル: Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution. 著者: Laura Bracun / Atsushi Yamagata / Bern M Christianson / Tohru Terada / Daniel P Canniffe / Mikako Shirouzu / Lu-Ning Liu / 要旨: The reaction center (RC)-light-harvesting complex 1 (LH1) supercomplex plays a pivotal role in bacterial photosynthesis. Many RC-LH1 complexes integrate an additional protein PufX that is key for ...The reaction center (RC)-light-harvesting complex 1 (LH1) supercomplex plays a pivotal role in bacterial photosynthesis. Many RC-LH1 complexes integrate an additional protein PufX that is key for bacterial growth and photosynthetic competence. Here, we present a cryo-electron microscopy structure of the RC-LH1-PufX supercomplex from at 2.8-Å resolution. The RC-LH1-PufX monomer contains an LH ring of 15 αβ-polypeptides with a 30-Å gap formed by PufX. PufX acts as a molecular "cross brace" to reinforce the RC-LH1 structure. The unusual PufX-mediated large opening in the LH1 ring and defined arrangement of proteins and cofactors provide the molecular basis for the assembly of a robust RC-LH1-PufX supercomplex and efficient quinone transport and electron transfer. These architectural features represent the natural strategies for anoxygenic photosynthesis and environmental adaptation.