登録情報 データベース : EMDB / ID : EMD-10513 構造の表示 ダウンロードとリンクタイトル Structure of the NDH-1MS complex from Thermosynechococcus elongatus マップデータStructure of the NDH-1MS complex from Thermosynechococcus elongatus 詳細 試料 詳細 機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
: / トランスロカーゼ; ヒドロンの輸送の触媒; 酸化還元酵素反応を伴う / photosynthetic electron transport chain / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / plasma membrane-derived thylakoid membrane / photosynthesis, light reaction / NADH dehydrogenase activity / mitochondrial respiratory chain complex I assembly / NADH dehydrogenase (ubiquinone) activity / quinone binding ... : / トランスロカーゼ; ヒドロンの輸送の触媒; 酸化還元酵素反応を伴う / photosynthetic electron transport chain / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / plasma membrane-derived thylakoid membrane / photosynthesis, light reaction / NADH dehydrogenase activity / mitochondrial respiratory chain complex I assembly / NADH dehydrogenase (ubiquinone) activity / quinone binding / electron transport coupled proton transport / ATP synthesis coupled electron transport / cell adhesion molecule binding / aerobic respiration / extracellular matrix organization / extracellular matrix / NAD binding / 4 iron, 4 sulfur cluster binding / membrane => GO:0016020 / cell adhesion / iron ion binding / extracellular space / plasma membrane 類似検索 - 分子機能 NAD(P)H-quinone oxidoreductase subunit 5, organellar chromatophore 2 / CO2 hydration / CO2 hydration protein (ChpXY) / NADH dehydrogenase-like complex, subunit S / NAD(P)H dehydrogenase subunit S / NAD(P)H-quinone oxidoreductase subunit O / Cyanobacterial and plant NDH-1 subunit O / NAD(P)H-quinone oxidoreductase subunit M / NAD(P)H-quinone oxidoreductase subunit L / NAD(P)H-quinone oxidoreductase, subunit N ... NAD(P)H-quinone oxidoreductase subunit 5, organellar chromatophore 2 / CO2 hydration / CO2 hydration protein (ChpXY) / NADH dehydrogenase-like complex, subunit S / NAD(P)H dehydrogenase subunit S / NAD(P)H-quinone oxidoreductase subunit O / Cyanobacterial and plant NDH-1 subunit O / NAD(P)H-quinone oxidoreductase subunit M / NAD(P)H-quinone oxidoreductase subunit L / NAD(P)H-quinone oxidoreductase, subunit N / Cyanobacterial and plastid NDH-1 subunit M / NADH dehydrogenase transmembrane subunit / NADH-quinone oxidoreductase cyanobacterial subunit N / NADH-plastoquinone oxidoreductase, subunit I / NAD(P)H-quinone oxidoreductase subunit 2, N-terminal / NAD(P)H-quinone oxidoreductase subunit 2 N-terminal / FAS1 domain / FAS1 domain superfamily / Fasciclin domain / FAS1/BIgH3 domain profile. / Four repeated domains in the Fasciclin I family of proteins, present in many other contexts. / NAD(P)H-quinone oxidoreductase subunit 3, bacterial/plastid / NAD(P)H-quinone oxidoreductase, subunit N/subunit 2 / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ / NADH dehydrogenase, subunit C / NADH-quinone oxidoreductase, chain M/4 / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / NADH-ubiquinone oxidoreductase chain 4L/K / NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 / NADH-ubiquinone/plastoquinone oxidoreductase chain 6 / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminal / NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH-ubiquinone oxidoreductase chain 4L/Mnh complex subunit C1-like / NADH-ubiquinone/plastoquinone oxidoreductase chain 4L / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / NADH:ubiquinone oxidoreductase / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / Proton-conducting membrane transporter / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / [NiFe]-hydrogenase, large subunit / 4Fe-4S dicluster domain / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain 類似検索 - ドメイン・相同性 NAD(P)H-quinone oxidoreductase subunit J / NAD(P)H-quinone oxidoreductase subunit 3 / NAD(P)H-quinone oxidoreductase subunit H / NAD(P)H-quinone oxidoreductase subunit N / Tlr0906 protein / NADH dehydrogenase subunit 4 / NADH dehydrogenase subunit 5 / NAD(P)H-quinone oxidoreductase subunit L / NAD(P)H-quinone oxidoreductase subunit K / NAD(P)H-quinone oxidoreductase subunit 4L ... NAD(P)H-quinone oxidoreductase subunit J / NAD(P)H-quinone oxidoreductase subunit 3 / NAD(P)H-quinone oxidoreductase subunit H / NAD(P)H-quinone oxidoreductase subunit N / Tlr0906 protein / NADH dehydrogenase subunit 4 / NADH dehydrogenase subunit 5 / NAD(P)H-quinone oxidoreductase subunit L / NAD(P)H-quinone oxidoreductase subunit K / NAD(P)H-quinone oxidoreductase subunit 4L / NADH-quinone oxidoreductase subunit J / NAD(P)H-quinone oxidoreductase subunit I / NAD(P)H-quinone oxidoreductase subunit 1 / Tlr0636 protein / NAD(P)H-quinone oxidoreductase subunit M / Tll0220 protein / NAD(P)H-quinone oxidoreductase subunit 2 / NAD(P)H-quinone oxidoreductase subunit O 類似検索 - 構成要素生物種 Thermosynechococcus elongatus BP-1 (バクテリア) / Thermosynechococcus elongatus (strain BP-1) (バクテリア)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.2 Å 詳細 データ登録者Schuller JM / Saura P / Thiemann J / Schuller SK / Gamiz-Hernandez AP / Kurisu G / Nowaczyk MM / Kaila VRI 資金援助 ドイツ, 4件 詳細 詳細を隠すOrganization Grant number 国 European Research Council (ERC) 715311 ドイツ German Research Foundation (DFG) 836/4-1 ドイツ German Research Foundation (DFG) 836/3-2 ドイツ German Research Foundation (DFG) 836/1-1 ドイツ
引用ジャーナル : Nat Commun / 年 : 2020タイトル : Redox-coupled proton pumping drives carbon concentration in the photosynthetic complex I.著者 : Jan M Schuller / Patricia Saura / Jacqueline Thiemann / Sandra K Schuller / Ana P Gamiz-Hernandez / Genji Kurisu / Marc M Nowaczyk / Ville R I Kaila / 要旨 : Photosynthetic organisms capture light energy to drive their energy metabolism, and employ the chemical reducing power to convert carbon dioxide (CO) into organic molecules. Photorespiration, ... Photosynthetic organisms capture light energy to drive their energy metabolism, and employ the chemical reducing power to convert carbon dioxide (CO) into organic molecules. Photorespiration, however, significantly reduces the photosynthetic yields. To survive under low CO concentrations, cyanobacteria evolved unique carbon-concentration mechanisms that enhance the efficiency of photosynthetic CO fixation, for which the molecular principles have remained unknown. We show here how modular adaptations enabled the cyanobacterial photosynthetic complex I to concentrate CO using a redox-driven proton-pumping machinery. Our cryo-electron microscopy structure at 3.2 Å resolution shows a catalytic carbonic anhydrase module that harbours a Zn active site, with connectivity to proton-pumping subunits that are activated by electron transfer from photosystem I. Our findings illustrate molecular principles in the photosynthetic complex I machinery that enabled cyanobacteria to survive in drastically changing CO conditions. 履歴 登録 2019年11月27日 - ヘッダ(付随情報) 公開 2020年2月19日 - マップ公開 2020年2月19日 - 更新 2020年12月2日 - 現状 2020年12月2日 処理サイト : PDBe / 状態 : 公開
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