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...

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Detalles Bibliográficos
Autores principales: Masrati, Gal, Mondal, Ramakanta, Rimon, Abraham, Kessel, Amit, Padan, Etana, Lindahl, Erik, Ben-Tal, Nir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2020
Materias:
Biological Sciences
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

Internet

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

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