Article
A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.
Biochemistry - 9 Jul 2013
Boehr David D, Schnell Jason R, McElheny Dan, Bae Sung-Hun, Duggan Brendan M, Benkovic Stephen J, Dyson H Jane, Wright Peter E
Abstract excerpt
Correlated networks of amino acids have been proposed to play a fundamental role in allostery and enzyme catalysis. These networks of amino acids can be traced from surface-exposed residues all the way into the active site, and disruption of these networks can decrease enzyme activity. Substitution of the distal Gly121 residue in Escherichia coli dihydrofolate reductase results in an up to 200-fold decrease in...
Topics
- Amino Acids
- Models, Molecular
- Mutation
- Nuclear Magnetic Resonance, Biomolecular
- Tetrahydrofolate Dehydrogenase