PloS one, 2011-11, Vol.6 (11), p.e26115-e26115
2011
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Characterization of the Na⁺/H⁺ antiporter from Yersinia pestis
- Ist Teil von
- PloS one, 2011-11, Vol.6 (11), p.e26115-e26115
- Ort / Verlag
- United States: Public Library of Science
- Erscheinungsjahr
- 2011
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1932-6203eISSN: 1932-6203DOI: 10.1371/journal.pone.0026115Titel-ID: cdi_plos_journals_1311931978
- Format
- –
- Schlagworte
- Amino Acid Sequence, Binding sites, Biological warfare, Biology, Cell Membrane - metabolism, Chemistry, Computer applications, Computer simulation, E coli, Epidemics, Escherichia coli, Fluorescence, Historical account, Homeostasis, Hydrogen-Ion Concentration, Ion Transport, Life sciences, Medicine, Membrane vesicles, Membranes, Models, Molecular, Molecular dynamics, Molecular Dynamics Simulation, Molecular Sequence Data, Molecular structure, Na+/H+-exchanging ATPase, Pandemics, pH effects, Physical properties, Plague - metabolism, Protein Conformation, Protein structure, Proteins, Quality, Sequence Homology, Amino Acid, Sodium-Hydrogen Exchangers - chemistry, Sodium-Hydrogen Exchangers - metabolism, Structure-function relationships, Substrate Specificity, Yersinia pestis, Yersinia pestis - metabolism