Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
The P-type ATPase subunit KdpB of KdpFABC hydrolyzes ATP while K+ transport was assumed to occur through channel-like subunit KdpA. Here, the authors show two cryo-EM structures of KdpFABC which suggest a translocation pathway through two inter-subunit half-channels formed by KdpA and KdpB.
Guardado en:
Autores principales: | C. Stock, L. Hielkema, I. Tascón, D. Wunnicke, G. T. Oostergetel, M. Azkargorta, C. Paulino, I. Hänelt |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/56ab652f6ae74938964ac89a3f6d6f3e |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC
por: Jakob M. Silberberg, et al.
Publicado: (2021) -
Publisher Correction: A c-di-AMP riboswitch controlling kdpFABC operon transcription regulates the potassium transporter system in Bacillus thuringiensis
por: Xun Wang, et al.
Publicado: (2019) -
Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin
por: Sarah J Piper, et al.
Publicado: (2019) -
Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex
por: Diego F. Gauto, et al.
Publicado: (2019) -
The cryo-EM structure of the bacterial flagellum cap complex suggests a molecular mechanism for filament elongation
por: Natalie S. Al-Otaibi, et al.
Publicado: (2020)