A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance

Bacterial disulfide isomerases shuffle incorrect disulfide bonds. Here, the authors structurally characterize the disulfide isomerase ScsC fromProteus mirabilisand identify a functionally important shape-shifting motif that allows ScsC to adopt a diverse range of conformations and enable swarming in...

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Autores principales:	Emily J. Furlong, Alvin W. Lo, Fabian Kurth, Lakshmanane Premkumar, Makrina Totsika, Maud E. S. Achard, Maria A. Halili, Begoña Heras, Andrew E. Whitten, Hassanul G. Choudhury, Mark A. Schembri, Jennifer L. Martin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8f04e6bca0c44df1aae8cb752f2ba122
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spelling	oai:doaj.org-article:8f04e6bca0c44df1aae8cb752f2ba1222021-12-02T14:42:44ZA shape-shifting redox foldase contributes to Proteus mirabilis copper resistance10.1038/ncomms160652041-1723https://doaj.org/article/8f04e6bca0c44df1aae8cb752f2ba1222017-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms16065https://doaj.org/toc/2041-1723Bacterial disulfide isomerases shuffle incorrect disulfide bonds. Here, the authors structurally characterize the disulfide isomerase ScsC fromProteus mirabilisand identify a functionally important shape-shifting motif that allows ScsC to adopt a diverse range of conformations and enable swarming in the presence of copper stress.Emily J. FurlongAlvin W. LoFabian KurthLakshmanane PremkumarMakrina TotsikaMaud E. S. AchardMaria A. HaliliBegoña HerasAndrew E. WhittenHassanul G. ChoudhuryMark A. SchembriJennifer L. MartinNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Emily J. Furlong Alvin W. Lo Fabian Kurth Lakshmanane Premkumar Makrina Totsika Maud E. S. Achard Maria A. Halili Begoña Heras Andrew E. Whitten Hassanul G. Choudhury Mark A. Schembri Jennifer L. Martin A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
description	Bacterial disulfide isomerases shuffle incorrect disulfide bonds. Here, the authors structurally characterize the disulfide isomerase ScsC fromProteus mirabilisand identify a functionally important shape-shifting motif that allows ScsC to adopt a diverse range of conformations and enable swarming in the presence of copper stress.
format	article
author	Emily J. Furlong Alvin W. Lo Fabian Kurth Lakshmanane Premkumar Makrina Totsika Maud E. S. Achard Maria A. Halili Begoña Heras Andrew E. Whitten Hassanul G. Choudhury Mark A. Schembri Jennifer L. Martin
author_facet	Emily J. Furlong Alvin W. Lo Fabian Kurth Lakshmanane Premkumar Makrina Totsika Maud E. S. Achard Maria A. Halili Begoña Heras Andrew E. Whitten Hassanul G. Choudhury Mark A. Schembri Jennifer L. Martin
author_sort	Emily J. Furlong
title	A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
title_short	A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
title_full	A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
title_fullStr	A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
title_full_unstemmed	A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
title_sort	shape-shifting redox foldase contributes to proteus mirabilis copper resistance
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/8f04e6bca0c44df1aae8cb752f2ba122
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A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance

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