Ontology type: schema:ScholarlyArticle Open Access: True
2016-08
AUTHORSSo-ichiro Nishiyama, Yohei Takahashi, Kentaro Yamamoto, Daisuke Suzuki, Yasuaki Itoh, Kazumasa Sumita, Yumiko Uchida, Michio Homma, Katsumi Imada, Ikuro Kawagishi
ABSTRACTVibrio cholerae, the etiological agent of cholera, was found to be attracted by taurine (2-aminoethanesulfonic acid), a major constituent of human bile. Mlp37, the closest homolog of the previously identified amino acid chemoreceptor Mlp24, was found to mediate taxis to taurine as well as L-serine, L-alanine, L-arginine, and other amino acids. Methylation of Mlp37 was enhanced upon the addition of taurine and amino acids. Isothermal titration calorimetry demonstrated that a purified periplasmic fragment of Mlp37 binds directly to taurine, L-serine, L-alanine and L-arginine. Crystal structures of the periplamic domain of Mlp37 revealed that L-serine and taurine bind to the membrane-distal PAS domain in essentially in the same way. The structural information was supported by characterising the in vivo properties of alanine-substituted mutant forms of Mlp37. The fact that the ligand-binding domain of the L-serine complex had a small opening, which would accommodate a larger R group, accounts for the broad ligand specificity of Mlp37 and allowed us to visualise ligand binding to Mlp37 with fluorescently labelled L-serine. Taken together, we conclude that Mlp37 serves as the major chemoreceptor for taurine and various amino acids. More... »
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RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/srep20866'
This table displays all metadata directly associated to this object as RDF triples.
325 TRIPLES
21 PREDICATES
85 URIs
34 LITERALS
22 BLANK NODES