Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.

Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP do...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Ariel E Mechaly, Nathalie Sassoon, Jean-Michel Betton, Pedro M Alzari
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/6b4ccaa2fcad46948266d02794ce5154
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:6b4ccaa2fcad46948266d02794ce5154
record_format	dspace
spelling	oai:doaj.org-article:6b4ccaa2fcad46948266d02794ce51542021-11-18T05:37:36ZSegmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.1544-91731545-788510.1371/journal.pbio.1001776https://doaj.org/article/6b4ccaa2fcad46948266d02794ce51542014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24492262/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK α-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states.Ariel E MechalyNathalie SassoonJean-Michel BettonPedro M AlzariPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 12, Iss 1, p e1001776 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Ariel E Mechaly Nathalie Sassoon Jean-Michel Betton Pedro M Alzari Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.
description	Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK α-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states.
format	article
author	Ariel E Mechaly Nathalie Sassoon Jean-Michel Betton Pedro M Alzari
author_facet	Ariel E Mechaly Nathalie Sassoon Jean-Michel Betton Pedro M Alzari
author_sort	Ariel E Mechaly
title	Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.
title_short	Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.
title_full	Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.
title_fullStr	Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.
title_full_unstemmed	Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.
title_sort	segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/6b4ccaa2fcad46948266d02794ce5154
work_keys_str_mv	AT arielemechaly segmentalhelicalmotionsanddynamicalasymmetrymodulatehistidinekinaseautophosphorylation AT nathaliesassoon segmentalhelicalmotionsanddynamicalasymmetrymodulatehistidinekinaseautophosphorylation AT jeanmichelbetton segmentalhelicalmotionsanddynamicalasymmetrymodulatehistidinekinaseautophosphorylation AT pedromalzari segmentalhelicalmotionsanddynamicalasymmetrymodulatehistidinekinaseautophosphorylation
_version_	1718424853098266624

Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.

Ejemplares similares