Cargando…
Mechanism of Na(+)-dependent citrate transport from the structure of an asymmetrical CitS dimer
The common human pathogen Salmonella enterica takes up citrate as a nutrient via the sodium symporter SeCitS. Uniquely, our 2.5 Å x-ray structure of the SeCitS dimer shows three different conformations of the active protomer. One protomer is in the outside-facing state. Two are in different inside-f...
Autores principales: | Wöhlert, David, Grötzinger, Maria J, Kühlbrandt, Werner, Yildiz, Özkan |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4718727/ https://www.ncbi.nlm.nih.gov/pubmed/26636752 http://dx.doi.org/10.7554/eLife.09375 |
Ejemplares similares
-
Structure and transport mechanism of the sodium/proton antiporter
MjNhaP1
por: Paulino, Cristina, et al.
Publicado: (2014) -
Structure and substrate ion binding in the sodium/proton antiporter
PaNhaP
por: Wöhlert, David, et al.
Publicado: (2014) -
Electrogenic Cation Binding in the Electroneutral Na(+)/H(+) Antiporter of Pyrococcus abyssi
por: Călinescu, Octavian, et al.
Publicado: (2016) -
Structural basis of proton translocation and force generation in mitochondrial ATP synthase
por: Klusch, Niklas, et al.
Publicado: (2017) -
Structural insights into the elevator-like mechanism of the sodium/citrate symporter CitS
por: Kim, Ji Won, et al.
Publicado: (2017)