Cargando…
HAMP Domain Rotation and Tilting Movements Associated with Signal Transduction in the PhoQ Sensor Kinase
HAMP domains are α-helical coiled coils that often transduce signals from extracytoplasmic sensing domains to cytoplasmic domains. Limited structural information has resulted in hypotheses that specific HAMP helix movement changes downstream enzymatic activity. These hypotheses were tested by mutage...
Autores principales: | Matamouros, Susana, Hager, Kyle R., Miller, Samuel I. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society of Microbiology
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4447245/ https://www.ncbi.nlm.nih.gov/pubmed/26015499 http://dx.doi.org/10.1128/mBio.00616-15 |
Ejemplares similares
-
Crystal Structure of a Functional Dimer of the PhoQ Sensor Domain
por: Cheung, Jonah, et al.
Publicado: (2008) -
Allosteric mechanism of signal transduction in the two-component system histidine kinase PhoQ
por: Mensa, Bruk, et al.
Publicado: (2021) -
Osmosensing by the bacterial PhoQ/PhoP two-component system
por: Yuan, Jing, et al.
Publicado: (2017) -
Assembly of the Transmembrane Domain of E. coli PhoQ Histidine Kinase: Implications for Signal Transduction from Molecular Simulations
por: Lemmin, Thomas, et al.
Publicado: (2013) -
Virulence and Stress Responses of Shigella flexneri Regulated by PhoP/PhoQ
por: Lin, Zhiwei, et al.
Publicado: (2018)