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Título

Structure of a chimeric EnvZ, visualizing histidine kinase autophosphorylation and deciphering cis-trans directionality

AutorMiguel-Romero, Laura ; Casino, Patricia ; Marina, Alberto
Fecha de publicación19-jun-2013
CitaciónXIIIth International Congress of SBE. International congress of the Spanish Biophysical Society (2013)
ResumenReversible protein phosphoryla1on is the most wide spread regulatory mechanism in signalt ransduc1on. In two-component systems, the main signal transduc1on mechanism in bacteria, the signaling process starts by the autophosphoryla1on of a conserved his1dine in the sensor his1dine kinase (HK). Transfer of the phosphoryl group from the HK his1dine to a conserved aspar1c of its cognate response regulator (RR) propagates the signal and triggers the cellular response. Prototypical HKs are membrane bound homodimers with two structurally conserved cytoplasmic domains: DHp, is formed by two long helices (α1 and α2) where α1 contains a phosphorylatable conserved His residue, and CA, which binds ATP. Autophosphoryla1on could either proceeds via cis-, the autophosphoryla1on occurs by an intra-subunit manner, like HK853, or trans- mechanism which implies an inter-subunit autophosphoryla1on, like EnvZ.
DescripciónPóster original presentado XIIIth International Congress of SBE. International congress of the Spanish Biophysical Society, celebrado en Valencia, 19-20 junio, 2013
URIhttp://hdl.handle.net/10261/123592
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