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Literature summary for 1.5.1.3 extracted from

  • Krahn, J.M.; Jackson, M.R.; DeRose, E.F.; Howell, E.E.; London, R.E.
    Crystal structure of a type II dihydrofolate reductase catalytic ternary complex (2007), Biochemistry, 46, 14878-14888.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
ternary complex of isoform R67 with dihydrofolate and NADPH, resolved to 1.26 A. In the catalytic complex, the polar backbone atoms of two symmetry-related I68 residues provide recognition motifs that interact with the carboxamide on the nicotinamide ring, and the N3-O4 amide function on the pteridine ring. This set of interactions orients the aromatic rings of substrate and cofactor in a relative endo geometry in which the reactive centers are held in close proximity. Additionally, a central, hydrogen-bonded network consisting of two pairs of Y69-Q67/Q67-Y69 residues provides a tight interface, which holds the substrates in place in an orientation conductive to hydride transfer Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00383 isozyme type II, R-plasmid encoded isoform R67
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Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli