The Quaternary Structure of the R-State of Escherichia coli Aspartate Transcarbamoylase in Solution Is Different from That in the Crystal and Is Modified by Mg2+·ATP Binding
Author:
Affiliation:
1. CERMES3, U. INSERM 988, CNRS UMR 8211, EHESS, Université Paris Descartes, BP 8, F-94801 Villejuif Cedex, France
2. Institut de Biologie Intégrative de la Cellule, UMR 9198, Université Paris-Sud, F-91405 Orsay Cedex, France
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00160
Reference9 articles.
1. Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate Transcarbamoylase
2. New Paradigm for Allosteric Regulation of Escherichia coli Aspartate Transcarbamoylase
3. A Second Allosteric Site in Escherichia coli Aspartate Transcarbamoylase
4. The Allosteric activator Mg-ATP Modifies the Quaternary Structure of the R-state of Escherichia coli Aspartate Transcarbamylase Without Altering the T↔R Equilibrium
5. CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates
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