The Allosteric activator Mg-ATP Modifies the Quaternary Structure of the R-state of Escherichia coli Aspartate Transcarbamylase Without Altering the T↔R Equilibrium
- 8 June 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 309 (3), 817-832
- https://doi.org/10.1006/jmbi.2001.4681
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- The Protein Data BankNucleic Acids Research, 2000
- Intramolecular signal transmission in enterobacterial aspartate transcarbamylases II. engineering co-operativity and allosteric regulation in the aspartate transcarbamylase of Erwinia herbicolaJournal of Molecular Biology, 1999
- CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic CoordinatesJournal of Applied Crystallography, 1995
- Determination of the regularization parameter in indirect-transform methods using perceptual criteriaJournal of Applied Crystallography, 1992
- Complex of N-phosphonacetyl-l-aspartate with aspartate carbamoyltransferaseJournal of Molecular Biology, 1988
- Homotropic effects in aspartate transcarbamoylaseJournal of Molecular Biology, 1985
- Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transitionJournal of Molecular Biology, 1979
- The nature of the altered allosteric behaviour of 2-thiouracil aspartate transcarbamylaseJournal of Molecular Biology, 1977
- Biosynthesis of Escherichia coli aspartate transcarbamylase: I. Parameters of gene expression and sequential biosynthesis of the subunitsJournal of Molecular Biology, 1972
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965