Chemotaxis of Vibrio cholerae is a complex process where multiple paralogues of various chemotaxis genes participate. V. cholerae contains five copies of the response regulator protein CheY (CheYV) and the role played by these CheY homologs in chemotaxis and virulence are investigated only through a few in vivo studies. As identification of the molecular features that discriminate CheYVs in terms of FliM binding is necessary for the detailed understanding of chemotaxis and pathogenesis, we built the models of CheYVs through comparative modeling and MD simulation was performed on each model in their phosphorylated and Mg+2 bound state. Our analysis identified the key structural elements, unique to CheY3V, which complement the N-terminal part of FliMV and we explained how the structure, shape, and surface properties of the FliM binding pocket of other CheYVs abrogate this function. Furthermore, we have provided the structural basis of a putative cross species interaction between CheYE and FliMV, identified in a recent in vivo study.
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