Cargando…
E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form
According to the traditional view, GTPases act as molecular switches, which cycle between distinct ‘on’ and ‘off’ conformations bound to GTP and GDP, respectively. Translation elongation factor EF-Tu is a GTPase essential for prokaryotic protein synthesis. In its GTP-bound form, EF-Tu delivers amino...
Autores principales: | Johansen, Jesper S, Kavaliauskas, Darius, Pfeil, Shawn H, Blaise, Mickaël, Cooperman, Barry S, Goldman, Yale E, Thirup, Søren S, Knudsen, Charlotte R |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6144822/ https://www.ncbi.nlm.nih.gov/pubmed/30107565 http://dx.doi.org/10.1093/nar/gky697 |
Ejemplares similares
-
Structural dynamics of translation elongation factor Tu during aa-tRNA delivery to the ribosome
por: Kavaliauskas, Darius, et al.
Publicado: (2018) -
EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways
por: Liu, Wei, et al.
Publicado: (2015) -
Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms
por: Simonetti, Angelita, et al.
Publicado: (2013) -
High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP
por: Schumacher, Maria A., et al.
Publicado: (2020) -
Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2
por: Dubiez, Etienne, et al.
Publicado: (2015)