Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/202900
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Conformational priming of RepA-WH1 for functional amyloid conversion detected by NMR spectroscopy |
Autor: | Pantoja-Uceda, D.; Oroz, Javier CSIC ORCID; Fernández, Cristina CSIC; Alba, Eva de CSIC; Giraldo, R. CSIC ORCID; Laurents, Douglas V. CSIC ORCID | Palabras clave: | Amyloidogenesis intermediates Conformational dynamics Functional bacterial amyloid Hydrogen/deuterium exchange Nuclear magnetic resonance |
Fecha de publicación: | 3-mar-2020 | Editor: | Elsevier | Citación: | Structure 28: 336–347 (2020) | Resumen: | How proteins with a stable globular fold acquire the amyloid state is still largely unknown. RepA, a versatile plasmidic DNA binding protein from Pseudomonas savastanoi, is functional as a transcriptional repressor or as an initiator or inhibitor of DNA replication, the latter via assembly of an amyloidogenic oligomer. Its N-terminal domain (WH1) is responsible for discrimination between these functional abilities by undergoing insufficiently understood structural changes. RepA-WH1 is a stable dimer whose conformational dynamics had not been explored. Here, we have studied it through NMR {1H}-15N relaxation and H/D exchange kinetics measurements. The N- and the C-terminal α-helices, and the internal amyloidogenic loop, are partially unfolded in solution. S4-indigo, a small inhibitor of RepA-WH1 amyloidogenesis, binds to and tethers the N-terminal α-helix to a β-hairpin that is involved in dimerization, thus providing evidence for a priming role of fraying ends and dimerization switches in the amyloidogenesis of folded proteins. | Descripción: | 29 p.-6 fig.-1 tab. | Versión del editor: | https://doi.org/10.1016/j.str.2019.12.007 | URI: | http://hdl.handle.net/10261/202900 | DOI: | 10.1016/j.str.2019.12.007 | ISSN: | 0969-2126 | E-ISSN: | 1878-4186 |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
Structure_Pantoja-Uceda_2020.pdf | Postprint | 8,05 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
5
checked on 20-abr-2024
WEB OF SCIENCETM
Citations
5
checked on 27-feb-2024
Page view(s)
225
checked on 24-abr-2024
Download(s)
107
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.