Reversible fold-switching controls the functional cycle of the antitermination factor RfaH

The antitermination factor RfaH adopts two functional states where its C-terminal domain is folded either as an α-helical hairpin or β-barrel. Here the authors employ solution state NMR measurements to show that the C-terminal domain transforms into the β-barrel only upon binding to the elongation c...

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Autores principales:	Philipp Konrad Zuber, Kristian Schweimer, Paul Rösch, Irina Artsimovitch, Stefan H. Knauer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/daefa0dcbec247efbb406bb9ab9188b3
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spelling	oai:doaj.org-article:daefa0dcbec247efbb406bb9ab9188b32021-12-02T16:57:55ZReversible fold-switching controls the functional cycle of the antitermination factor RfaH10.1038/s41467-019-08567-62041-1723https://doaj.org/article/daefa0dcbec247efbb406bb9ab9188b32019-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08567-6https://doaj.org/toc/2041-1723The antitermination factor RfaH adopts two functional states where its C-terminal domain is folded either as an α-helical hairpin or β-barrel. Here the authors employ solution state NMR measurements to show that the C-terminal domain transforms into the β-barrel only upon binding to the elongation complex and refolds back after dissociation.Philipp Konrad ZuberKristian SchweimerPaul RöschIrina ArtsimovitchStefan H. KnauerNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Philipp Konrad Zuber Kristian Schweimer Paul Rösch Irina Artsimovitch Stefan H. Knauer Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
description	The antitermination factor RfaH adopts two functional states where its C-terminal domain is folded either as an α-helical hairpin or β-barrel. Here the authors employ solution state NMR measurements to show that the C-terminal domain transforms into the β-barrel only upon binding to the elongation complex and refolds back after dissociation.
format	article
author	Philipp Konrad Zuber Kristian Schweimer Paul Rösch Irina Artsimovitch Stefan H. Knauer
author_facet	Philipp Konrad Zuber Kristian Schweimer Paul Rösch Irina Artsimovitch Stefan H. Knauer
author_sort	Philipp Konrad Zuber
title	Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
title_short	Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
title_full	Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
title_fullStr	Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
title_full_unstemmed	Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
title_sort	reversible fold-switching controls the functional cycle of the antitermination factor rfah
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/daefa0dcbec247efbb406bb9ab9188b3
work_keys_str_mv	AT philippkonradzuber reversiblefoldswitchingcontrolsthefunctionalcycleoftheantiterminationfactorrfah AT kristianschweimer reversiblefoldswitchingcontrolsthefunctionalcycleoftheantiterminationfactorrfah AT paulrosch reversiblefoldswitchingcontrolsthefunctionalcycleoftheantiterminationfactorrfah AT irinaartsimovitch reversiblefoldswitchingcontrolsthefunctionalcycleoftheantiterminationfactorrfah AT stefanhknauer reversiblefoldswitchingcontrolsthefunctionalcycleoftheantiterminationfactorrfah
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Reversible fold-switching controls the functional cycle of the antitermination factor RfaH

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