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6EU6

Sensor Amt Protein

6EU6 の概要
エントリーDOI10.2210/pdb6eu6/pdb
分子名称Ammonium transporter, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, nonyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside, ... (7 entities in total)
機能のキーワードammonium transporter, signalling, histidine kinase, membrane protein
由来する生物種Kuenenia stuttgartiensis
タンパク質・核酸の鎖数1
化学式量合計44965.46
構造登録者
Pflueger, T.,Hernandez, C.,Andrade, S.L.A. (登録日: 2017-10-28, 公開日: 2018-01-24, 最終更新日: 2024-01-17)
主引用文献Pfluger, T.,Hernandez, C.F.,Lewe, P.,Frank, F.,Mertens, H.,Svergun, D.,Baumstark, M.W.,Lunin, V.Y.,Jetten, M.S.M.,Andrade, S.L.A.
Signaling ammonium across membranes through an ammonium sensor histidine kinase.
Nat Commun, 9:164-164, 2018
Cited by
PubMed Abstract: Sensing and uptake of external ammonium is essential for anaerobic ammonium-oxidizing (anammox) bacteria, and is typically the domain of the ubiquitous Amt/Rh ammonium transporters. Here, we report on the structure and function of an ammonium sensor/transducer from the anammox bacterium "Candidatus Kuenenia stuttgartiensis" that combines a membrane-integral ammonium transporter domain with a fused histidine kinase. It contains a high-affinity ammonium binding site not present in assimilatory Amt proteins. The levels of phosphorylated histidine in the kinase are coupled to the presence of ammonium, as conformational changes during signal recognition by the Amt module are transduced internally to modulate the kinase activity. The structural analysis of this ammonium sensor by X-ray crystallography and small-angle X-ray-scattering reveals a flexible, bipartite system that recruits a large uptake transporter as a sensory module and modulates its functionality to achieve a mechanistic coupling to a kinase domain in order to trigger downstream signaling events.
PubMed: 29323112
DOI: 10.1038/s41467-017-02637-3
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.98 Å)
構造検証レポート
Validation report summary of 6eu6
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2026-04-22に公開中

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