5AVF

The ligand binding domain of Mlp37 with taurine

Summary for 5AVF

• Entry DOI: 10.2210/pdb5avf/pdb
• Related: 3c8c 5AVE
• Descriptor: Methyl-accepting chemotaxis (MCP) signaling domain protein, 2-AMINOETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: chemoreceptor, ligand complex, mcp-like protein, pas-like domain, signaling protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 2
• Total formula weight: 56585.11

Authors

Takahashi, Y.,Sumita, K.,Uchida, Y.,Nishiyama, S.,Kawagishi, I.,Imada, K. (deposition date: 2015-06-15, release date: 2016-06-01, Last modification date: 2023-11-08)

Primary citation

Nishiyama, S.,Takahashi, Y.,Yamamoto, K.,Suzuki, D.,Itoh, Y.,Sumita, K.,Uchida, Y.,Homma, M.,Imada, K.,Kawagishi, I.
Identification of a Vibrio cholerae chemoreceptor that senses taurine and amino acids as attractants
Sci Rep, 6:20866-20866, 2016

PubMed Abstract: 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.

PubMed: 26878914
DOI: 10.1038/srep20866

Experimental method

X-RAY DIFFRACTION (1.95 Å)