Cargando…
Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
Histidine is a versatile residue playing key roles in enzyme catalysis thanks to the chemistry of its imidazole group that can serve as nucleophile, general acid or base depending on its protonation state. In bacteria, signal transduction relies on two-component systems (TCS) which comprise a sensor...
Autores principales: | Mideros-Mora, Cristina, Miguel-Romero, Laura, Felipe-Ruiz, Alonso, Casino, Patricia, Marina, Alberto |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7005713/ https://www.ncbi.nlm.nih.gov/pubmed/32034139 http://dx.doi.org/10.1038/s41467-020-14540-5 |
Ejemplares similares
-
Author Correction: Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
por: Mideros-Mora, Cristina, et al.
Publicado: (2020) -
A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases
por: Liu, Yixiang, et al.
Publicado: (2017) -
Genetic and Biochemical Dissection of a HisKA Domain Identifies Residues Required Exclusively for Kinase and Phosphatase Activities
por: Willett, Jonathan W., et al.
Publicado: (2012) -
Structure-based pKa prediction provides a thermodynamic basis for the role of histidines in pH-induced conformational transitions in dengue virus
por: Chaudhury, Sidhartha, et al.
Publicado: (2015) -
Histidine Protonation and Conformational Switching in Diphtheria Toxin Translocation Domain
por: Rodnin, Mykola V., et al.
Publicado: (2023)