9kpj
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Helicobacter pylori chemoreceptor TlpA ligand-binding domain in complex with indole== | |
| + | <StructureSection load='9kpj' size='340' side='right'caption='[[9kpj]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9kpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_PMSS1 Helicobacter pylori PMSS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KPJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IND:INDOLE'>IND</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9kpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9kpj OCA], [https://pdbe.org/9kpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9kpj RCSB], [https://www.ebi.ac.uk/pdbsum/9kpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kpj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Indole has recently been recognized as a ubiquitous interspecies and interkingdom signaling molecule. However, the mechanisms underlying indole sensing in prokaryotes remain largely uncharacterized, and direct binding of indole to bacterial extracellular sensors has not been demonstrated. In this study, we show that the Helicobacter pylori chemoreceptor TlpA, which plays an important role in the host colonization by this gastric pathogen, binds indole and several related compounds, including menadione, through its dCache sensory domain. This binding occurs in the physiological range of indole concentrations and elicits a repellent response. The repellent response to indole mediated by the sensory domain of TlpA was also observed for the chimeric TlpA-Tar receptor in Escherichia coli. While ligands typically bind to the membrane-distal pocket of dCache domains, our structural and biochemical analyses demonstrate that indole binds to the membrane-proximal pocket of TlpA dCache. The TlpA-mediated negative chemotaxis of H. pylori correlates with the inhibitory effects of indole on bacterial growth and biofilm formation. The dCache domain of TlpA thus represents a new high-affinity sensory module for indole and related compounds that may be widespread in bacteria and play an important role in the physiology and pathogenicity of H. pylori. | ||
| - | + | Discovery of an indole-sensing chemoreceptor in Helicobacter pylori.,Wang X, Xu W, Yao F, Liu S, Zhang Y, Sourjik V, Bi S Curr Biol. 2025 Oct 20;35(20):5018-5032.e6. doi: 10.1016/j.cub.2025.09.021. Epub , 2025 Sep 30. PMID:41033314<ref>PMID:41033314</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9kpj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori PMSS1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bi SY]] | ||
| + | [[Category: Wang X]] | ||
Current revision
Crystal structure of Helicobacter pylori chemoreceptor TlpA ligand-binding domain in complex with indole
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