Radical Redesign of a Tandem Array of Four R67 Dihydrofolate Reductase Genes Yields a Functional, Folded Protein Possessing 45 Substitutions
Author:
Affiliation:
1. Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi1005943
Reference70 articles.
1. Current status of the aadA and dfr gene cassette families
2. Searching Sequence Space: Two Different Approaches to Dihydrofolate Reductase Catalysis
3. A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site
4. Crystal Structure of a Type II Dihydrofolate Reductase Catalytic Ternary Complex
5. High-resolution structure of a plasmid-encoded dihydrofolate reductase: pentagonal network of water molecules in theD2-symmetric active site
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