ISSN: 2332-0737
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Vibrio cholarae is the causative agent of cholera. It is responsible behind a variety of diseases specifically the multidrug-resistant nosocomial infections and chronic lung infections in cystic fibrosis patients. One of the vital genes of the organism responsible for its multidrug resistant behaviour is the gene PA3523 which codes for the multidrug efflux transporter. The expression of PA3523 is regulated by the dimeric transcription factor Lrp having Helix-Turn-Helix DNA binding motif. So far there have been no previous reports that depict the characterization of Lrp protein from Vibrio cholerae from a structural point of view. In the present work, an attempt has been made to characterize Lrp protein by structural bioinformatics approach. The dimeric structure of Lrp was built by comparative modelling technique. The dimeric model of Lrp was then docked on to the corresponding promoter region of the PA3523 gene encoding the multidrug efflux transporter. The docked complex of promoter DNA with Lrp protein was subjected to molecular dynamics simulations to identify the mode of DNA protein interactions. So far, this is the first report that depicts the mechanistic details of gene regulation by Lrp protein. This work may therefore be useful to illuminate the still obscure molecular mechanism behind disease propagation by Vibrio cholerae