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