Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 3, Pages 288-U70Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1978
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Funding
- Canadian Institutes of Health Research (CIHR)
- CIHR
- Natural Sciences and Engineering Research Council of Canada
- Canada Foundation for Innovation
- Ministere de la Recherche, de la Science et de la Technologie du Quebec
- McGill University
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Allostery has been studied for many decades, yet it remains challenging to determine experimentally how it occurs at a molecular level. We have developed an approach combining isothermal titration calorimetry, circular dichroism and nuclear magnetic resonance spectroscopy to quantify allostery in terms of protein thermodynamics, structure and dynamics. This strategy was applied to study the interaction between aminoglycoside N-(6')-acetyltransferase-Ii and one of its substrates, acetyl coenzyme A. It was found that homotropic allostery between the two active sites of the homodimeric enzyme is modulated by opposing mechanisms. One follows a classical Koshland-Nemethy-Filmer (KNF) paradigm, whereas the other follows a recently proposed mechanism in which partial unfolding of the subunits is coupled to ligand binding. Competition between folding, binding and conformational changes represents a new way to govern energetic communication between binding sites.
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