The influence of ATP on the binding of aromatic amino acids to the ligand response domain of the tyrosine repressor of Haemophilus influenzae
Open Access
- 2 February 2000
- journal article
- Published by Wiley in FEBS Letters
- Vol. 467 (1), 87-90
- https://doi.org/10.1016/s0014-5793(00)01118-2
Abstract
The binding of aromatic amino acids to the ligand response domain of the tyrosine repressor (TyrR) protein (TyrRlrd) of Haemophilus influenzae was investigated using circular dichroism and fluorescence spectroscopy. The induced secondary structural changes were unique for each aromatic amino acid and were further influenced by the presence or absence of ATP. Tyrosine was found to have the highest affinity for TyrRlrd in the absence of ATP, whereas the affinity for ATP itself increased in the presence of tyrosine. Binding of tyrosine is therefore the conformational trigger for the activation of TyrR whereas ATP is regarded as a conformational co‐activator.Keywords
This publication has 18 references indexed in Scilit:
- X-ray structure and conformational dynamics of the HIV-1 protease in complex with the inhibitor SDZ283-910: agreement of time-resolved spectroscopy and molecular dynamics simulationsJournal of Molecular Biology, 1999
- Sensitivity of Flavin Fluorescence Dynamics in Neuronal Nitric Oxide Synthase to Cofactor-Induced Conformational Changes and DimerizationBiochemistry, 1998
- Thermodynamics of the Interaction of the Escherichia coli Regulatory Protein TyrR with DNA Studied by Fluorescence SpectroscopyBiochemistry, 1998
- The ProDom database of protein domain familiesNucleic Acids Research, 1998
- Expression, Purification, and Functional Analysis of the TyrR Protein ofHaemophilus influenzaeProtein Expression and Purification, 1997
- Characterization of the Interaction between RhoGDI and Cdc42Hs Using Fluorescence SpectroscopyPublished by Elsevier ,1996
- Kinetics of Nucleotide-Induced Changes in the Tryptophan Fluorescence of the Molecular Chaperone Hsc70 and Its Subfragments Suggest the ATP-Induced Conformational Change Follows Initial ATP BindingBiochemistry, 1995
- Prediction of Protein Secondary Structure at Better than 70% AccuracyJournal of Molecular Biology, 1993
- A Self-Consistent Method for the Analysis of Protein Secondary Structure from Circular DichroismAnalytical Biochemistry, 1993
- TyrR protein of Escherichia coli and its role as repressor and activatorMolecular Microbiology, 1991