The Central Domain of Escherichia coli TyrR Is Responsible for Hexamerization Associated with Tyrosine-mediated Repression of Gene Expression
Open Access
- 1 June 2002
- journal article
- Published by Elsevier
- Vol. 277 (26), 23186-23192
- https://doi.org/10.1074/jbc.m112184200
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- The Influence of ATP on the Association and Unfolding of the Tyrosine Repressor Ligand Response Domain of Haemophilus influenzaeBiochemical and Biophysical Research Communications, 2001
- Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. ThorntonJournal of Molecular Biology, 2000
- Diffusing Probe Measurements of Polystyrene Latex Particles in Polyelectrolyte Solutions: Deviations from Stokes−Einstein BehaviorMacromolecules, 1999
- Solution structure of the DNA-binding domain of NtrC with three alanine substitutionsJournal of Molecular Biology, 1999
- Association states of the transcription activator protein NtrC from E. coli determined by analytical ultracentrifugationJournal of Molecular Biology, 1998
- Effector‐induced self‐association and conformational changes in the enhancer‐binding protein NTRCMolecular Microbiology, 1996
- Constitutive Forms of the Enhancer-binding Protein NtrC: Evidence that Essential Oligomerization Determinants Lie in the Central Activation DomainJournal of Molecular Biology, 1995
- Ligand-induced Self-association of the Escherichia coli Regulatory Protein TyrRJournal of Molecular Biology, 1994
- Prediction of Protein Secondary Structure at Better than 70% AccuracyJournal of Molecular Biology, 1993
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976