1DHR

CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE

Summary for 1DHR

• Entry DOI: 10.2210/pdb1dhr/pdb
• Descriptor: DIHYDROPTERIDINE REDUCTASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase(acting on nadh or nadph)
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 26242.60

Authors

Varughese, K.I.,Skinner, M.M.,Whiteley, J.M.,Matthews, D.A.,Xuong, N.H. (deposition date: 1992-03-30, release date: 1993-07-15, Last modification date: 2024-02-07)

Primary citation

Varughese, K.I.,Skinner, M.M.,Whiteley, J.M.,Matthews, D.A.,Xuong, N.H.
Crystal structure of rat liver dihydropteridine reductase.
Proc.Natl.Acad.Sci.USA, 89:6080-6084, 1992

PubMed Abstract: The structure of a binary complex of dihydropteridine reductase [DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7] with its cofactor, NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR is an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in the human enzyme is associated with severe symptoms of a variant form of phenylketonuria and maps to a tightly linked sequence of secondary-structural elements near the dimer interface. Dimerization is mediated by a four-helix bundle motif (two helices from each protomer) having an unusual right-handed twist. DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase.

PubMed: 1631094
DOI: 10.1073/pnas.89.13.6080

Experimental method

X-RAY DIFFRACTION (2.3 Å)