3UB9

Periplasmic portion of the Helicobacter pylori chemoreceptor TlpB with hydroxyurea bound

3UB9 の概要

• エントリーDOI: 10.2210/pdb3ub9/pdb
• 関連するPDBエントリー: 3UB6 3UB7 3UB8
• 分子名称: chemoreceptor TlpB, N-HYDROXYUREA, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: homodimer, four-helix bundle, pas domain, membrane protein
• 由来する生物種: Helicobacter pylori
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42275.80

構造登録者

Henderson, J.N.,Sweeney, E.G.,Goers, J.,Wreden, C.,Hicks, K.G.,Parthasarathy, R.,Guillemin, K.J.,Remington, S.J. (登録日: 2011-10-23, 公開日: 2012-06-27, 最終更新日: 2024-02-28)

主引用文献

Goers Sweeney, E.,Henderson, J.N.,Goers, J.,Wreden, C.,Hicks, K.G.,Foster, J.K.,Parthasarathy, R.,Remington, S.J.,Guillemin, K.
Structure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpB.
Structure, 20:1177-1188, 2012

PubMed Abstract: pH sensing is crucial for survival of most organisms, yet the molecular basis of such sensing is poorly understood. Here, we present an atomic resolution structure of the periplasmic portion of the acid-sensing chemoreceptor, TlpB, from the gastric pathogen Helicobacter pylori. The structure reveals a universal signaling fold, a PAS domain, with a molecule of urea bound with high affinity. Through biophysical, biochemical, and in vivo mutagenesis studies, we show that urea and the urea-binding site residues play critical roles in the ability of H. pylori to sense acid. Our signaling model predicts that protonation events at Asp114, affected by changes in pH, dictate the stability of TlpB through urea binding.

PubMed: 22705207
DOI: 10.1016/j.str.2012.04.021

実験手法

X-RAY DIFFRACTION (1.42 Å)