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Crystallization of the bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase domain of the human trifunctional enzyme
Author(s) -
Allaire Marc,
Li Yunge,
Mejia Narciso R.,
Pelletier Joelle N.,
MacKenzie Robert E.,
Cygler Miroslaw
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199612)26:4<479::aid-prot9>3.0.co;2-6
Subject(s) - crystallization , phosphofructokinase 2 , enzyme , dehydrogenase , methylenetetrahydrofolate reductase , chemistry , biochemistry , gene , organic chemistry , genotype
Abstract Methylenetetrahydrofolate([H 4 ] folate) dehydrogenase (D) and methenyl[H 4 ] folate cyclohydrolase (C) coexist as a bifunctional enzyme (DC) or as the amino‐terminal domain of a trifunctional enzyme (DCS) where the third activity is 10‐formyl[H 4 ]lfolate synthetase (S). Two crystal forms of the DC domain of the human cytosolic DCS enzyme have been grown from polyethyleneglycol solution. The monoclinic P2 1 crystals diffract to 2.8 Å with a = 72.5 Å, b = 68.5 Å, c = 125.2 Å, and β = 91.8° but were found to be twinned. The orthorhombic P2 1 2 1 2 1 crystals diffract to 2.5 Å with a = 67.7 Å, b = 135.9 Å, c = 61.6 Å, and contain two molecules per asymmetric unit. Proteins 26:479–480 © 1996 Wiley‐Liss, Inc.