2NUU

Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex

2NUU の概要

• エントリーDOI: 10.2210/pdb2nuu/pdb
• 分子名称: Ammonia channel, Nitrogen regulatory protein P-II 2, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: membrane protein complex, nitrogen regulation, ammonia transport, transport protein-signaling protein complex, transport protein/signaling protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P69681
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 336606.55

構造登録者

Conroy, M.J.,Durand, A.,Lupo, D.,Li, X.-D.,Bullough, P.A.,Winkler, F.K.,Merrick, M. (登録日: 2006-11-09, 公開日: 2006-11-21, 最終更新日: 2023-10-25)

主引用文献

Conroy, M.J.,Durand, A.,Lupo, D.,Li, X.-D.,Bullough, P.A.,Winkler, F.K.,Merrick, M.
The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel
Proc.Natl.Acad.Sci.Usa, 104:1213-1218, 2007

PubMed Abstract: Amt proteins are ubiquitous channels for the conduction of ammonia in archaea, eubacteria, fungi, and plants. In Escherichia coli, previous studies have indicated that binding of the PII signal transduction protein GlnK to the ammonia channel AmtB regulates the channel thereby controlling ammonium influx in response to the intracellular nitrogen status. Here, we describe the crystal structure of the complex between AmtB and GlnK at a resolution of 2.5 A. This structure of PII in a complex with one of its targets reveals physiologically relevant conformations of both AmtB and GlnK. GlnK interacts with AmtB almost exclusively via a long surface loop containing Y51 (T-loop), the tip of which inserts deeply into the cytoplasmic pore exit, blocking ammonia conduction. Y51 of GlnK is also buried in the pore exit, explaining why uridylylation of this residue prevents complex formation.

PubMed: 17220269
DOI: 10.1073/pnas.0610348104

実験手法

X-RAY DIFFRACTION (2.5 Å)