Crystallographic investigation of the cooperative interaction between trimethoprim, reduced cofactor and dihydrofolate reductase.

Journal article

The structure of the complex between E. coli (RT500) form I dihydrofolate reductase, the antibacterial trimethoprim and NADPH has been determined by X-ray crystallography. The inhibitor and cofactor are in mutual contact. A flexible chain segment which includes Met 20 is in contact with the inhibitor in the presence of NADPH, but more distant in its absence. By contrast, the inhibitor conformation is little changed with NADPH present. We discuss these observations with regard to the mutually ...

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Authors: Champness, J; Stammers, D; Beddell, C

• Publication status: Published
• Journal: FEBS letters
• Volume: 199
• Issue: 1
• Pages: 61-67
• Publication date: 1986-04-01
• DOI: 10.1016/0014-5793(86)81224-8
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Escherichia coli; Models, Molecular; X-Ray Diffraction; Binding Sites; Protein Conformation; NADP; Trimethoprim; Tetrahydrofolate Dehydrogenase; Lactobacillus casei