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Crystallization of the bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase domain of the human trifunctional enzyme.

作者信息

Allaire M, Li Y, Mejia N R, Pelletier J N, MacKenzie R E, Cygler M

机构信息

Institut de Recherche en Biotechnologie, Conseil National de Recherche du Canada, Montréal, Québec, Canada.

出版信息

Proteins. 1996 Dec;26(4):479-80. doi: 10.1002/(SICI)1097-0134(199612)26:4<479::AID-PROT9>3.0.CO;2-6.

DOI:10.1002/(SICI)1097-0134(199612)26:4<479::AID-PROT9>3.0.CO;2-6
PMID:8990501
Abstract

Methylenetetrahydrofolate([H4] folate) dehydrogenase (D) and methenyl[H4] 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[H4]folate 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 A with a = 72.5 A, b = 68.5 A, c = 125.2 A, and beta = 91.8 degrees but were found to be twinned. The orthorhombic P2(1)2(1)2(1) crystals diffract to 2.5 A with a = 67.7 A, b = 135.9 A, c = 61.6 A, and contain two molecules per asymmetric unit.

摘要

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