Structure and Proposed Mechanism for the pH-Sensing Helicobacter pylori Chemoreceptor TlpB
| Autor: | Raghuveer Parthasarathy, John Goers, J. Nathan Henderson, Kevin G. Hicks, Christopher Wreden, S. James Remington, Karen Guillemin, Emily Goers Sweeney, Jeneva K. Foster |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Chemoreceptor Molecular Sequence Data Receptors Cell Surface Plasma protein binding Biology Crystallography X-Ray Protein Structure Secondary Article 03 medical and health sciences Protein structure Bacterial Proteins Structural Biology PAS domain Escherichia coli Urea Amino Acid Sequence Binding site Molecular Biology 030304 developmental biology 0303 health sciences Binding Sites Urea binding Helicobacter pylori Protein Stability 030306 microbiology Periplasmic space Hydrogen-Ion Concentration Recombinant Proteins Protein Structure Tertiary 3. Good health Biochemistry Mutation Protons Signal transduction Dimerization Sequence Alignment Plasmids Protein Binding Signal Transduction |
| Zdroj: | Structure. 20:1177-1188 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2012.04.021 |
| Popis: | SummarypH 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|