期刊
STRUCTURE
卷 20, 期 7, 页码 1177-1188出版社
CELL PRESS
DOI: 10.1016/j.str.2012.04.021
关键词
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资金
- National Institutes of Health, National Research Service [R01 DK075667, A1091098-02]
- National Institutes of Health
- MCB [208731]
- National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1021374] Funding Source: National Science Foundation
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 pylon. 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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