English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/124444
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Título

Visualizing autophosphorylation in histidine kinases

AutorCasino, Patricia ; Miguel-Romero, Laura ; Marina, Alberto
Fecha de publicación6-feb-2014
EditorNature Publishing Group
CitaciónNature Communications 5: 3258 (2014)
ResumenReversible 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.
DescripciónCorrigendum at: Nature Communications 5, Article number: 3645 doi:10.1038/ncomms4645. Published 14 April 2014
Versión del editorhttp://dx.doi.org/10.1038/ncomms4258
http://dx.doi.org/10.1038/ncomms4645
URIhttp://hdl.handle.net/10261/124444
DOI10.1038/ncomms4258
10.1038/ncomms4645
Identificadoresissn: 2041-1723
Aparece en las colecciones: (IBV) Artículos
(IBMB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
ncomms4258_PCasino.pdf2,46 MBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.