Crystal structure of chicken liver dihydrofolate reductase complexed with NAPD super(+) and biopterin

The 2.2-angstrom crystal structure of chicken liver dihydrofolate reductase (EC 1.5.1.3, DHFR) has been solved as a ternary complex with NADP super(+) and biopterin (a poor substrate). The space group and unit cell are isomorphous with the previously reported structure of chicken liver DHFR complexe...

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Bibliographic Details
Published inBiochemistry (Easton) Vol. 31; no. 32; pp. 7264 - 7273
Main Authors McTigue, MA, Davies, JF II, Kaufman, B T, Kraut, J
Format Journal Article
LanguageEnglish
Published 01.01.1992
Subjects
biopterin
chickens
complex
crystal structure
dihydrofolate reductase
liver
NADP super(+)
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Summary:The 2.2-angstrom crystal structure of chicken liver dihydrofolate reductase (EC 1.5.1.3, DHFR) has been solved as a ternary complex with NADP super(+) and biopterin (a poor substrate). The space group and unit cell are isomorphous with the previously reported structure of chicken liver DHFR complexed with NADPH and phenyltriazine. The structure contains an ordered water molecule hydrogen-bonded to both hydroxyls of the biopterin dihydroxypropyl group as well as to O4 and N5 of the biopterin pteridine ring. This water molecule, not observed in previously determined DHFR structures, is positioned to complete a proposed route for proton transfer from the side-chain carboxylate of E30 to N5 of the pteridine ring.
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ISSN:0006-2960