2NS1

Crystal structure of the e. coli ammonia channel AMTB complexed with the signal transduction protein GLNK

2NS1 の概要

• エントリーDOI: 10.2210/pdb2ns1/pdb
• 関連するPDBエントリー: 1GNK 1U7G 1XQF 2B2H 2GNK
• 分子名称: Ammonia channel, Nitrogen regulatory protein P-II 2, octyl beta-D-glucopyranoside, ... (6 entities in total)
• 機能のキーワード: protein-protein complex, membrane protein, ammonia, channel, regulatory, inhibitor, signal protein, adp, bog, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, 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: 2
• 化学式量合計: 58521.21

構造登録者

Gruswitz, F.,O'Connell III, J.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (登録日: 2006-11-02, 公開日: 2006-12-26, 最終更新日: 2023-08-30)

主引用文献

Gruswitz, F.,O'Connell III, J.,Stroud, R.M.
Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96
Proc.Natl.Acad.Sci.USA, 104:42-47, 2007

PubMed Abstract: Ammonia conductance is highly regulated. A P(II) signal transduction protein, GlnK, is the final regulator of transmembrane ammonia conductance by the ammonia channel AmtB in Escherichia coli. The complex formed between AmtB and inhibitory GlnK at 1.96-A resolution shows that the trimeric channel is blocked directly by GlnK and how, in response to intracellular nitrogen status, the ability of GlnK to block the channel is regulated by uridylylation/deuridylylation at Y51. ATP and Mg(2+) augment the interaction of GlnK. The hydrolyzed product, adenosine 5'-diphosphate orients the surface of GlnK for AmtB blockade. 2-Oxoglutarate diminishes AmtB/GlnK association, and sites for 2-oxoglutarate are evaluated.

PubMed: 17190799
DOI: 10.1073/pnas.0609796104

実験手法

X-RAY DIFFRACTION (1.962 Å)