Abstract
Yersinia pestis, the bacterium that historically accounts for the Black Death epidemics, has nowadays gained new attention as a possible biological warfare agent. In this study, its NA +/H + antiporter is investigated for the first time, by a combination of experimental and computational methodologies. We determined the protein's substrate specificity and pH dependence by fluorescence measurements in everted membrane vesicles. Subsequently, we constructed a model of the protein's structure and validated the model using molecular dynamics simulations. Taken together, better understanding of the Yersinia pestis NA +/H + antiporter's structure-function relationship may assist in studies on ion transport, mechanism of action and designing specific blockers of NA +/H + antiporter to help in fighting Yersinia pestis -associated infections. We hope that our model will prove useful both from mechanistic and pharmaceutical perspectives. © 2011 Ganoth et al.
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CITATION STYLE
Ganoth, A., Alhadeff, R., Kohen, D., & Arkin, I. T. (2011). Characterization of the NA +/H + antiporter from Yersinia pestis. PLoS ONE, 6(11). https://doi.org/10.1371/journal.pone.0026115
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