Uncoupling conformational states from activity in an allosteric enzyme

Active and inactive state ATP-phosphoribosyltransferases (ATP-PRTs) are believed to have different conformations. Here the authors show that in both states, ATP-PRT has a similar structural arrangement, suggesting that dynamic alterations are involved in ATP-PRT regulation by allosteric modulators.

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Autores principales:	João P. Pisco, Cesira de Chiara, Kamila J. Pacholarz, Acely Garza-Garcia, Roksana W. Ogrodowicz, Philip A. Walker, Perdita E. Barran, Stephen J. Smerdon, Luiz Pedro S. de Carvalho
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/603702800eb7417086645e28e6a8150e
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spelling	oai:doaj.org-article:603702800eb7417086645e28e6a8150e2021-12-02T14:16:04ZUncoupling conformational states from activity in an allosteric enzyme10.1038/s41467-017-00224-02041-1723https://doaj.org/article/603702800eb7417086645e28e6a8150e2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00224-0https://doaj.org/toc/2041-1723Active and inactive state ATP-phosphoribosyltransferases (ATP-PRTs) are believed to have different conformations. Here the authors show that in both states, ATP-PRT has a similar structural arrangement, suggesting that dynamic alterations are involved in ATP-PRT regulation by allosteric modulators.João P. PiscoCesira de ChiaraKamila J. PacholarzAcely Garza-GarciaRoksana W. OgrodowiczPhilip A. WalkerPerdita E. BarranStephen J. SmerdonLuiz Pedro S. de CarvalhoNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q João P. Pisco Cesira de Chiara Kamila J. Pacholarz Acely Garza-Garcia Roksana W. Ogrodowicz Philip A. Walker Perdita E. Barran Stephen J. Smerdon Luiz Pedro S. de Carvalho Uncoupling conformational states from activity in an allosteric enzyme
description	Active and inactive state ATP-phosphoribosyltransferases (ATP-PRTs) are believed to have different conformations. Here the authors show that in both states, ATP-PRT has a similar structural arrangement, suggesting that dynamic alterations are involved in ATP-PRT regulation by allosteric modulators.
format	article
author	João P. Pisco Cesira de Chiara Kamila J. Pacholarz Acely Garza-Garcia Roksana W. Ogrodowicz Philip A. Walker Perdita E. Barran Stephen J. Smerdon Luiz Pedro S. de Carvalho
author_facet	João P. Pisco Cesira de Chiara Kamila J. Pacholarz Acely Garza-Garcia Roksana W. Ogrodowicz Philip A. Walker Perdita E. Barran Stephen J. Smerdon Luiz Pedro S. de Carvalho
author_sort	João P. Pisco
title	Uncoupling conformational states from activity in an allosteric enzyme
title_short	Uncoupling conformational states from activity in an allosteric enzyme
title_full	Uncoupling conformational states from activity in an allosteric enzyme
title_fullStr	Uncoupling conformational states from activity in an allosteric enzyme
title_full_unstemmed	Uncoupling conformational states from activity in an allosteric enzyme
title_sort	uncoupling conformational states from activity in an allosteric enzyme
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/603702800eb7417086645e28e6a8150e
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Uncoupling conformational states from activity in an allosteric enzyme

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