Cargando…
Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA
[Image: see text] The detailed mechanism of ATP hydrolysis in ATP-binding cassette (ABC) transporters is still not fully understood. Here, we employed (31)P solid-state NMR to probe the conformational changes and dynamics during the catalytic cycle by locking the multidrug ABC transporter BmrA in pr...
Autores principales: | Lacabanne, Denis, Wiegand, Thomas, Di Cesare, Margot, Orelle, Cédric, Ernst, Matthias, Jault, Jean-Michel, Meier, Beat H., Böckmann, Anja |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9284561/ https://www.ncbi.nlm.nih.gov/pubmed/35776907 http://dx.doi.org/10.1021/jacs.2c04287 |
Ejemplares similares
-
Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA from Bacillus subtilis
por: Lacabanne, Denis, et al.
Publicado: (2019) -
Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies
por: Kunert, Britta, et al.
Publicado: (2014) -
Stubborn Contaminants: Influence of Detergents on the Purity of the Multidrug ABC Transporter BmrA
por: Wiseman, Benjamin, et al.
Publicado: (2014) -
Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state
por: Pérez Carrillo, Victor Hugo, et al.
Publicado: (2022) -
Unfolding Individual Domains of BmrA, a Bacterial ABC Transporter Involved in Multidrug Resistance
por: Oepen, Kristin, et al.
Publicado: (2023)