PDB ID: 1DHI

Long-range structural effects in a second-site revertant of a mutant dihydrofolate reductase.

Brown, K.A.,Howell, E.E.,Kraut, J.
(1993)  Proc.Natl.Acad.Sci.USA  90 : 11753 - 11756

PubMed: 8265622
DOI: 10.1073/pnas.90.24.11753

How Do Mutation at Phenylalanine-153 and Isoleucine-155 Partially Suppress the Effects of the Aspartate-27-> Serine Mutation in Escherichia Coli Dihydrofolate Reductase

Dion, A.,Linn, C.E.,Bradrick, T.D.  et al.
(1993)  Biochemistry  32 : 3479

Role of Aspartate 27 of Dihydrofolate Reductase from Escherichia Coli in Interconversion of Active and Inactive Enzyme Conformers and the Binding of Nadph

Appleman, J.R.,Howell, E.E.,Kraut, J.  et al.
(1990)  J.Biol.Chem.  265 : 5579

A Second-Site Mutation at Phenylalanine-137 that Increases Catalytic Efficiency in the Mutant Aspartate-27-> Serine Escherichia Coli Dihydrofolate Reductase

Howell, E.E.,Booth, C.,Farnum, M.  et al.
(1990)  Biochemistry  29 : 8561

Dihydrofolate Reductase from Escherichia Coli: Probing the Role of Aspartate-27 and Phenylalanine-137 in Enzyme Conformation and the Binding of Nadph

Dunn, S.M.,Lanigan, T.M.,Howell, E.E.
(1990)  Biochemistry  29 : 8569

Functional Role of Aspartic Acid-27 in Dihydrofolate Reductase Revealed by Mutagenesis

Howell, E.E.,Villafranca, J.E.,Waren, M.S.  et al.
(1986)  Science  231 : 1123

Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase at 1.7 Angstroms Resolution. I. General Features and Binding of Methotrexate

Bolin, J.T.,Filman, D.J.,Matthews, D.A.  et al.
(1982)  Biochemistry  257 : 13650

Crystal Structures of Escherichia Coli and Lactobacillus Casei Dihydrofolate Reductase at 1.7 Angstroms Resolution. II. Environment of Bound Nadph and Implications for Catalysis

Filman, D.J.,Bolin, J.T.,Matthews, D.A.  et al.
(1982)  J.Biol.Chem.  257 : 13663