Uncoupling conformational states from activity in an allosteric enzyme

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.

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2017-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-00224-0

Internet

https://doi.org/10.1038/s41467-017-00224-0

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