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An angular motion of a conserved four-helix bundle facilitates alternating access transport in the TtNapA and EcNhaA transporters
There is ongoing debate regarding the mechanism through which cation/proton antiporters (CPAs), like Thermus thermophilus NapA (TtNapA) and Escherichia coli NapA (EcNhaA), alternate between their outward- and inward-facing conformations in the membrane. CPAs comprise two domains, and it is unclear w...
| Autores principales: | , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
National Academy of Sciences
2020
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7749304/ https://www.ncbi.nlm.nih.gov/pubmed/33257549 http://dx.doi.org/10.1073/pnas.2002710117 |