Structure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpB.
Structure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpB.
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DOI：
10.1016/j.str.2012.04.021
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发表时间：
2012-07-03
期刊：
影响因子：
5.7
通讯作者：
Guillemin, Karen
中科院分区：
文献类型：
--
作者：
Sweeney, Emily Goers;Henderson, J. Nathan;Goers, John;Wreden, Christopher;Hicks, Kevin G.;Foster, Jeneva K.;Parthasarathy, Raghuveer;Remington, S. James;Guillemin, Karen
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.
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影响因子：
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作者：
Howitt MR;Lee JY;Lertsethtakarn P;Vogelmann R;Joubert LM;Ottemann KM;Amieva MR
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Amieva MR
DOI：
10.1073/pnas.90.12.5791
发表时间：
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