Cargando…
The dynamic dimer structure of the chaperone Trigger Factor
The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, the spatial arrangement of this dimeric chaperone storage form has remained unclear. Here, we determine its structure by a combination of high-resolution...
Autores principales: | Morgado, Leonor, Burmann, Björn M., Sharpe, Timothy, Mazur, Adam, Hiller, Sebastian |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5722895/ https://www.ncbi.nlm.nih.gov/pubmed/29222465 http://dx.doi.org/10.1038/s41467-017-02196-7 |
Ejemplares similares
-
Regulation of chaperone function by coupled folding and oligomerization
por: Mas, Guillaume, et al.
Publicado: (2020) -
A molecular mechanism of chaperone-client recognition
por: He, Lichun, et al.
Publicado: (2016) -
α-Synuclein regulation by chaperones in mammalian cells
por: Burmann, Björn M., et al.
Publicado: (2019) -
Keeping α-Synuclein at Bay: A More Active Role of Molecular Chaperones in Preventing Mitochondrial Interactions and Transition to Pathological States?
por: Aspholm, Emelie E., et al.
Publicado: (2020) -
Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins
por: Kawale, Ashish A., et al.
Publicado: (2021)