Article
Role of Lys-32 residues in R67 dihydrofolate reductase probed by asymmetric mutations.
The Journal of biological chemistry - 5 Nov 2004
Hicks Stephanie N, Smiley R Derike, Stinnett Lori G, Minor Kenneth H, Howell Elizabeth E
Abstract excerpt
R67 dihydrofolate reductase (R67 DHFR) is a novel protein encoded by an R-plasmid that confers resistance to the antibiotic, trimethoprim. This homotetrameric enzyme possesses 222 symmetry, which imposes numerous constraints on the single active site pore, including a "one-site-fits-both" strategy for binding its ligands, dihydrofolate (DHF) and NADPH. Previous studies uncovered salt effects on binding and...
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