5WBF
Double CACHE (dCACHE) sensing domain of TlpC chemoreceptor from Helicobacter pylori
5WBF の概要
| エントリーDOI | 10.2210/pdb5wbf/pdb |
| 分子名称 | Methyl-accepting chemotaxis transducer (TlpC), LACTIC ACID, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | bacterial protein, chemoreceptor sensing domain, double-cache domain, helicobacter pylori, signaling protein |
| 由来する生物種 | Helicobacter pylori |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 92170.72 |
| 構造登録者 | Machuca, M.A.,Johnson, K.S.,Liu, Y.C.,Steer, D.L.,Ottemann, K.M.,Roujeinikova, A. (登録日: 2017-06-28, 公開日: 2017-11-08, 最終更新日: 2023-11-15) |
| 主引用文献 | Machuca, M.A.,Johnson, K.S.,Liu, Y.C.,Steer, D.L.,Ottemann, K.M.,Roujeinikova, A. Helicobacter pylori chemoreceptor TlpC mediates chemotaxis to lactate. Sci Rep, 7:14089-14089, 2017 Cited by PubMed Abstract: It is recently appreciated that many bacterial chemoreceptors have ligand-binding domains (LBD) of the dCACHE family, a structure with two PAS-like subdomains, one membrane-proximal and the other membrane-distal. Previous studies had implicated only the membrane-distal subdomain in ligand recognition. Here, we report the 2.2 Å resolution crystal structure of dCACHE LBD of the Helicobacter pylori chemoreceptor TlpC. H. pylori tlpC mutants are outcompeted by wild type during stomach colonisation, but no ligands had been mapped to this receptor. The TlpC dCACHE LBD has two PAS-like subdomains, as predicted. The membrane-distal one possesses a long groove instead of a small, well-defined pocket. The membrane-proximal subdomain, in contrast, had a well-delineated pocket with a small molecule that we identified as lactate. We confirmed that amino acid residues making contact with the ligand in the crystal structure-N213, I218 and Y285 and Y249-were required for lactate binding. We determined that lactate is an H. pylori chemoattractant that is sensed via TlpC with a K = 155 µM. Lactate is utilised by H. pylori, and our work suggests that this pathogen seeks out lactate using chemotaxis. Furthermore, our work suggests that dCACHE domain proteins can utilise both subdomains for ligand recognition. PubMed: 29075010DOI: 10.1038/s41598-017-14372-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.19 Å) |
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