Cargando…
Conformational Selection Underlies Recognition of a Molybdoenzyme by Its Dedicated Chaperone
Molecular recognition is central to all biological processes. Understanding the key role played by dedicated chaperones in metalloprotein folding and assembly requires the knowledge of their conformational ensembles. In this study, the NarJ chaperone dedicated to the assembly of the membrane-bound r...
Autores principales: | Lorenzi, Magali, Sylvi, Léa, Gerbaud, Guillaume, Mileo, Elisabetta, Halgand, Frédéric, Walburger, Anne, Vezin, Hervé, Belle, Valérie, Guigliarelli, Bruno, Magalon, Axel |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3501500/ https://www.ncbi.nlm.nih.gov/pubmed/23185350 http://dx.doi.org/10.1371/journal.pone.0049523 |
Ejemplares similares
-
Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism
por: Arias-Cartin, Rodrigo, et al.
Publicado: (2016) -
History of Maturation of Prokaryotic Molybdoenzymes—A Personal View
por: Magalon, Axel
Publicado: (2023) -
In-cell investigation of the conformational landscape of the GTPase UreG by SDSL-EPR
por: Pierro, Annalisa, et al.
Publicado: (2023) -
Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy
por: Le Breton, Nolwenn, et al.
Publicado: (2015) -
The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
por: Neumann, Meina, et al.
Publicado: (2011)