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9LEG

AMO complex

これはPDB形式変換不可エントリーです。
9LEG の概要
エントリーDOI10.2210/pdb9leg/pdb
EMDBエントリー63025
分子名称Ammonia monooxygenase subunit A, COPPER (II) ION, [(2~{S})-2-hexadecanoyloxy-3-[methoxy(oxidanyl)phosphoryl]oxy-propyl] hexadecanoate, ... (13 entities in total)
機能のキーワードamo complex, membrane protein
由来する生物種Nitrosomonas halophila
詳細
タンパク質・核酸の鎖数15
化学式量合計393058.70
構造登録者
Li, Z.Q.,Yang, X.Y. (登録日: 2025-01-07, 公開日: 2026-02-04)
主引用文献Yang, X.,Li, Z.,Mao, T.Q.,Ma, C.,Chen, G.H.,Dong, H.P.,Sui, S.F.
Structural insights into the catalytic mechanism of ammonia monooxygenase.
Nat Commun, 17:508-508, 2025
Cited by
PubMed Abstract: Ammonia monooxygenase (AMO) oxidizes ammonia to hydroxylamine. Limited knowledge of the structural information of AMO hinders our understanding of the molecular mechanism underlying ammonia oxidation, impacting the mitigation of greenhouse gas emissions and enhancing agricultural productivity using ammonium as a nitrogen source. Herein, we report the cryo-electron microscopy structure of the AMO complex from an isolated strain of ammonia-oxidizing bacteria (AOB). AMO is a cylinder-shaped homotrimeric assembly composed of five subunits. A single-transmembrane protein and a soluble protein are potentially crucial in signal transduction during ammonia oxidation and mediating interactions with the outer membrane protein assembly machinery. Three modeled coppers, along with an adjacent water-mediated hydrogen-bond network, may facilitate an efficient proton transfer pathway from the periplasmic Cu to the active site Cu within the inner membrane, where Cu and Cu will act in concert to catalyze substrate reaction. The distinctive surface charge characteristics of AMO provide valuable insights into the structural features that govern ammonium assimilation and material transport during ammonia oxidation. These findings shed light on the molecular complexities of AMO and provides a structural foundation for elucidating the catalytic mechanism of ammonia oxidation.
PubMed: 41387732
DOI: 10.1038/s41467-025-67194-6
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.36 Å)
構造検証レポート
Validation report summary of 9leg
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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