4EXO

Revised, rerefined crystal structure of PDB entry 2QHK, methyl accepting chemotaxis protein

4EXO の概要

• エントリーDOI: 10.2210/pdb4exo/pdb
• 分子名称: Methyl-accepting chemotaxis protein, PYRUVIC ACID (3 entities in total)
• 機能のキーワード: signaling protein, chemotaxis receptor, pas domain, four helix bundle, methyl accepting chemotaxis receptor, periplasmic domain
• 由来する生物種: Vibrio parahaemolyticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16741.31

構造登録者

Sweeney, E.G.,Henderson, J.N.,Goers, J.,Wreden, C.,Hicks, K.G.,Foster, J.K.,Parthasarathy, R.,Remington, S.J.,Guillemin, K. (登録日: 2012-04-30, 公開日: 2012-05-30, 最終更新日: 2024-11-06)

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 (1.9 Å)