Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/124444
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Visualizing autophosphorylation in histidine kinases |
Autor: | Casino, Patricia CSIC ORCID; Miguel-Romero, Laura CSIC ORCID; Marina, Alberto CSIC ORCID | Fecha de publicación: | 6-feb-2014 | Editor: | Nature Publishing Group | Citación: | Nature Communications 5: 3258 (2014) | Resumen: | Reversible protein phosphorylation is the most widespread regulatory mechanism in signal transduction. Autophosphorylation in a dimeric sensor histidine kinase is the first step in two-component signalling, the predominant signal-transduction device in bacteria. Despite being the most abundant sensor kinases in nature, the molecular bases of the histidine kinase autophosphorylation mechanism are still unknown. Furthermore, it has been demonstrated that autophosphorylation can occur in two directions, cis (intrasubunit) or trans (intersubunit) within the dimeric histidine kinase. Here, we present the crystal structure of the complete catalytic machinery of a chimeric histidine kinase. The structure shows an asymmetric histidine kinase dimer where one subunit is caught performing the autophosphorylation reaction. A structure-guided functional analysis on HK853 and EnvZ, two prototypical cis- and trans-phosphorylating histidine kinases, has allowed us to decipher the catalytic mechanism of histidine kinase autophosphorylation, which seems to be common independently of the reaction directionality. | Descripción: | Corrigendum at: Nature Communications 5, Article number: 3645 doi:10.1038/ncomms4645. Published 14 April 2014 | Versión del editor: | http://dx.doi.org/10.1038/ncomms4258 http://dx.doi.org/10.1038/ncomms4645 |
URI: | http://hdl.handle.net/10261/124444 | DOI: | 10.1038/ncomms4258 10.1038/ncomms4645 |
Identificadores: | issn: 2041-1723 |
Aparece en las colecciones: | (IBV) Artículos (IBMB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
ncomms4258_PCasino.pdf | 2,46 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
104
checked on 10-abr-2024
WEB OF SCIENCETM
Citations
93
checked on 26-feb-2024
Page view(s)
403
checked on 23-abr-2024
Download(s)
381
checked on 23-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.