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Uncoupling conformational states from activity in an allosteric enzyme
- Source :
- Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
- Publication Year :
- 2017
- Publisher :
- Nature Portfolio, 2017.
-
Abstract
- 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.
- Subjects :
- Science
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 8
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Nature Communications
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.603702800eb7417086645e28e6a8150e
- Document Type :
- article
- Full Text :
- https://doi.org/10.1038/s41467-017-00224-0