Cargando…
Evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism
The ubiquitous P-loop fold nucleoside triphosphatases (NTPases) are typically activated by an arginine or lysine ‘finger’. Some of the apparently ancestral NTPases are, instead, activated by potassium ions. To clarify the activation mechanism, we combined comparative structure analysis with molecula...
Autores principales: | Shalaeva, Daria N, Cherepanov, Dmitry A, Galperin, Michael Y, Golovin, Andrey V, Mulkidjanian, Armen Y |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6310460/ https://www.ncbi.nlm.nih.gov/pubmed/30526846 http://dx.doi.org/10.7554/eLife.37373 |
Ejemplares similares
-
Common Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphatases
por: Kozlova, Maria I., et al.
Publicado: (2022) -
Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases—United in Diversity
por: Kozlova, Maria I., et al.
Publicado: (2022) -
Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins
por: Shalaeva, Daria N., et al.
Publicado: (2015) -
Modeling of interaction between cytochrome c and the WD domains of Apaf-1: bifurcated salt bridges underlying apoptosome assembly
por: Shalaeva, Daria N., et al.
Publicado: (2015) -
Emergence of cytochrome bc complexes in the context of photosynthesis
por: Dibrova, Daria V., et al.
Publicado: (2017)