Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

Bacterial two-component systems are composed of a sensor histidine kinase (HK) and an effector response regulator and upon signal detection, the HK autophosphorylates a conserved His residue. Here the authors structurally and functionally characterise two HKs, HK853–RR468 and EnvZ–OmpR, and find tha...

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Autores principales:	Cristina Mideros-Mora, Laura Miguel-Romero, Alonso Felipe-Ruiz, Patricia Casino, Alberto Marina
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a680d0f7de9a49d3bb3359801876a0f3
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spelling	oai:doaj.org-article:a680d0f7de9a49d3bb3359801876a0f32021-12-02T16:56:32ZRevisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases10.1038/s41467-020-14540-52041-1723https://doaj.org/article/a680d0f7de9a49d3bb3359801876a0f32020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14540-5https://doaj.org/toc/2041-1723Bacterial two-component systems are composed of a sensor histidine kinase (HK) and an effector response regulator and upon signal detection, the HK autophosphorylates a conserved His residue. Here the authors structurally and functionally characterise two HKs, HK853–RR468 and EnvZ–OmpR, and find that the rotamer of the phosphorylatable catalytic His is not influenced by the environmental pH, ruling out an earlier proposed pH-gated model.Cristina Mideros-MoraLaura Miguel-RomeroAlonso Felipe-RuizPatricia CasinoAlberto MarinaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Cristina Mideros-Mora Laura Miguel-Romero Alonso Felipe-Ruiz Patricia Casino Alberto Marina Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
description	Bacterial two-component systems are composed of a sensor histidine kinase (HK) and an effector response regulator and upon signal detection, the HK autophosphorylates a conserved His residue. Here the authors structurally and functionally characterise two HKs, HK853–RR468 and EnvZ–OmpR, and find that the rotamer of the phosphorylatable catalytic His is not influenced by the environmental pH, ruling out an earlier proposed pH-gated model.
format	article
author	Cristina Mideros-Mora Laura Miguel-Romero Alonso Felipe-Ruiz Patricia Casino Alberto Marina
author_facet	Cristina Mideros-Mora Laura Miguel-Romero Alonso Felipe-Ruiz Patricia Casino Alberto Marina
author_sort	Cristina Mideros-Mora
title	Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_short	Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_full	Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_fullStr	Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_full_unstemmed	Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
title_sort	revisiting the ph-gated conformational switch on the activities of hiska-family histidine kinases
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/a680d0f7de9a49d3bb3359801876a0f3
work_keys_str_mv	AT cristinamiderosmora revisitingthephgatedconformationalswitchontheactivitiesofhiskafamilyhistidinekinases AT lauramiguelromero revisitingthephgatedconformationalswitchontheactivitiesofhiskafamilyhistidinekinases AT alonsofeliperuiz revisitingthephgatedconformationalswitchontheactivitiesofhiskafamilyhistidinekinases AT patriciacasino revisitingthephgatedconformationalswitchontheactivitiesofhiskafamilyhistidinekinases AT albertomarina revisitingthephgatedconformationalswitchontheactivitiesofhiskafamilyhistidinekinases
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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

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