Janet S Finer-Moore
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Tryptophan 80 and leucine 143 are critical for the hydride transfer step of thymidylate synthase by controlling active site access.
Mutant forms of thymidylate synthase (TS) with substitutions at the conserved active site residue, Trp 80, are deficient in the hydride transfer step of the TS reaction. These mutants produce a… Expand
Structural basis for recognition of polyglutamyl folates by thymidylate synthase.
Thymidylate synthase (TS) catalyzes the final step in the de novo synthesis of thymidine. In vivo TS binds a polyglutamyl cofactor, polyglutamyl methylenetetrahydrofolate (CH2-H4folate), which serves… Expand
THE STRUCTURE OF ACUMYCIN: A 16-MEMBERED RING MACROLIDE ANTIBIOTIC
The structure of acumycin, an antibiotic isolated from Streptomyces griseoflavus, was determined from spectroscopic and X-ray studies. Acumycin was found to be a 16-member ring macrolide with two… Expand
Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate.
Title Cofactor-mediated conformational control in the bifunctional kinase / RNase Ire 1 Permalink
Background: Ire1 is a signal transduction protein in the endoplasmic reticulum (ER) membrane that serves to adjust the protein-folding capacity of the ER according to the needs of the cell. Ire1… Expand