The relationship between folding and activity in UreG, an intrinsically disordered enzyme

Abstract A growing body of literature on intrinsically disordered proteins (IDPs) led scientists to rethink the structure-function paradigm of protein folding. Enzymes are often considered an exception to the rule of intrinsic disorder (ID), believed to require a unique structure for catalysis. Howe...

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Autores principales:	Marta Palombo, Alessio Bonucci, Emilien Etienne, Stefano Ciurli, Vladimir N. Uversky, Bruno Guigliarelli, Valérie Belle, Elisabetta Mileo, Barbara Zambelli
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a1b925d80cc8421faa70d4865663e6ce
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spelling	oai:doaj.org-article:a1b925d80cc8421faa70d4865663e6ce2021-12-02T11:53:10ZThe relationship between folding and activity in UreG, an intrinsically disordered enzyme10.1038/s41598-017-06330-92045-2322https://doaj.org/article/a1b925d80cc8421faa70d4865663e6ce2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06330-9https://doaj.org/toc/2045-2322Abstract A growing body of literature on intrinsically disordered proteins (IDPs) led scientists to rethink the structure-function paradigm of protein folding. Enzymes are often considered an exception to the rule of intrinsic disorder (ID), believed to require a unique structure for catalysis. However, recent studies revealed the presence of disorder in several functional native enzymes. In the present work, we address the importance of dynamics for catalysis, by investigating the relationship between folding and activity in Sporosarcina pasteurii UreG (SpUreG), a P-loop GTPase and the first discovered native ID enzyme, involved in the maturation of the nickel-containing urease. The effect of denaturants and osmolytes on protein structure and activity was analyzed using circular dichroism (CD), Site-Directed Spin Labeling (SDSL) coupled to EPR spectroscopy, and enzymatic assays. Our data show that SpUreG needs a “flexibility window” to be catalytically competent, with both too low and too high mobility being detrimental for its activity.Marta PalomboAlessio BonucciEmilien EtienneStefano CiurliVladimir N. UverskyBruno GuigliarelliValérie BelleElisabetta MileoBarbara ZambelliNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marta Palombo Alessio Bonucci Emilien Etienne Stefano Ciurli Vladimir N. Uversky Bruno Guigliarelli Valérie Belle Elisabetta Mileo Barbara Zambelli The relationship between folding and activity in UreG, an intrinsically disordered enzyme
description	Abstract A growing body of literature on intrinsically disordered proteins (IDPs) led scientists to rethink the structure-function paradigm of protein folding. Enzymes are often considered an exception to the rule of intrinsic disorder (ID), believed to require a unique structure for catalysis. However, recent studies revealed the presence of disorder in several functional native enzymes. In the present work, we address the importance of dynamics for catalysis, by investigating the relationship between folding and activity in Sporosarcina pasteurii UreG (SpUreG), a P-loop GTPase and the first discovered native ID enzyme, involved in the maturation of the nickel-containing urease. The effect of denaturants and osmolytes on protein structure and activity was analyzed using circular dichroism (CD), Site-Directed Spin Labeling (SDSL) coupled to EPR spectroscopy, and enzymatic assays. Our data show that SpUreG needs a “flexibility window” to be catalytically competent, with both too low and too high mobility being detrimental for its activity.
format	article
author	Marta Palombo Alessio Bonucci Emilien Etienne Stefano Ciurli Vladimir N. Uversky Bruno Guigliarelli Valérie Belle Elisabetta Mileo Barbara Zambelli
author_facet	Marta Palombo Alessio Bonucci Emilien Etienne Stefano Ciurli Vladimir N. Uversky Bruno Guigliarelli Valérie Belle Elisabetta Mileo Barbara Zambelli
author_sort	Marta Palombo
title	The relationship between folding and activity in UreG, an intrinsically disordered enzyme
title_short	The relationship between folding and activity in UreG, an intrinsically disordered enzyme
title_full	The relationship between folding and activity in UreG, an intrinsically disordered enzyme
title_fullStr	The relationship between folding and activity in UreG, an intrinsically disordered enzyme
title_full_unstemmed	The relationship between folding and activity in UreG, an intrinsically disordered enzyme
title_sort	relationship between folding and activity in ureg, an intrinsically disordered enzyme
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/a1b925d80cc8421faa70d4865663e6ce
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The relationship between folding and activity in UreG, an intrinsically disordered enzyme

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