5avf: Difference between revisions
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The | ==The ligand binding domain of Mlp37 with taurine== | ||
<StructureSection load='5avf' size='340' side='right' caption='[[5avf]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5avf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AVF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AVF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAU:2-AMINOETHANESULFONIC+ACID'>TAU</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ave|5ave]], [[3c8c|3c8c]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5avf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avf OCA], [http://pdbe.org/5avf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5avf RCSB], [http://www.ebi.ac.uk/pdbsum/5avf PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vibrio 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. | |||
Identification of a Vibrio cholerae chemoreceptor that senses taurine and amino acids as attractants.,Nishiyama S, Takahashi Y, Yamamoto K, Suzuki D, Itoh Y, Sumita K, Uchida Y, Homma M, Imada K, Kawagishi I Sci Rep. 2016 Feb 16;6:20866. doi: 10.1038/srep20866. PMID:26878914<ref>PMID:26878914</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5avf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Imada, K]] | |||
[[Category: Kawagishi, I]] | |||
[[Category: Nishiyama, S]] | |||
[[Category: Sumita, K]] | [[Category: Sumita, K]] | ||
[[Category: Takahashi, Y]] | [[Category: Takahashi, Y]] | ||
[[Category: Uchida, Y]] | [[Category: Uchida, Y]] | ||
[[Category: Chemoreceptor]] | |||
[[Category: Ligand complex]] | |||
[[Category: Mcp-like protein]] | |||
[[Category: Pas-like domain]] | |||
[[Category: Signaling protein]] | |||
