- EMDB-33245: Cryo-EM structure of Na+-pumping NADH-ubiquinone oxidoreductase f... -
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基本情報
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データベース: EMDB / ID: EMD-33245
タイトル
Cryo-EM structure of Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae, with aurachin D-42
マップデータ
Na -NQR with AD42
試料
複合体: Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae, with aurachin D-42
タンパク質・ペプチド: x 6種
リガンド: x 9種
機能・相同性
機能・相同性情報
riboflavin binding / NADH:ubiquinone reductase (Na+-transporting) / Gram-negative-bacterium-type cell wall / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / sodium ion transport / FAD binding / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / transmembrane transport / FMN binding ...riboflavin binding / NADH:ubiquinone reductase (Na+-transporting) / Gram-negative-bacterium-type cell wall / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / sodium ion transport / FAD binding / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / transmembrane transport / FMN binding / electron transfer activity / metal ion binding / plasma membrane 類似検索 - 分子機能
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R01-AI132580
米国
引用
ジャーナル: Nat Commun / 年: 2022 タイトル: Cryo-EM structures of Na-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae. 著者: Jun-Ichi Kishikawa / Moe Ishikawa / Takahiro Masuya / Masatoshi Murai / Yuki Kitazumi / Nicole L Butler / Takayuki Kato / Blanca Barquera / Hideto Miyoshi / 要旨: The Na-pumping NADH-ubiquinone oxidoreductase (Na-NQR) couples electron transfer from NADH to ubiquinone with Na-pumping, generating an electrochemical Na gradient that is essential for energy- ...The Na-pumping NADH-ubiquinone oxidoreductase (Na-NQR) couples electron transfer from NADH to ubiquinone with Na-pumping, generating an electrochemical Na gradient that is essential for energy-consuming reactions in bacteria. Since Na-NQR is exclusively found in prokaryotes, it is a promising target for highly selective antibiotics. However, the molecular mechanism of inhibition is not well-understood for lack of the atomic structural information about an inhibitor-bound state. Here we present cryo-electron microscopy structures of Na-NQR from Vibrio cholerae with or without a bound inhibitor at 2.5- to 3.1-Å resolution. The structures reveal the arrangement of all six redox cofactors including a herein identified 2Fe-2S cluster located between the NqrD and NqrE subunits. A large part of the hydrophilic NqrF is barely visible in the density map, suggesting a high degree of flexibility. This flexibility may be responsible to reducing the long distance between the 2Fe-2S centers in NqrF and NqrD/E. Two different types of specific inhibitors bind to the N-terminal region of NqrB, which is disordered in the absence of inhibitors. The present study provides a foundation for understanding the function of Na-NQR and the binding manner of specific inhibitors.