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

✍ Scribed by Allaire, Marc; Li, Yunge; Mejia, Narciso R.; Pelletier, Joelle N.; MacKenzie, Robert E.; Cygler, Miroslaw

• Book ID: 101228433
• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 224 KB
• Volume: 26
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199612)26:4<479::aid-prot9>3.0.co;2-6

✦ Synopsis

Methylenetetrahydrofolate([H41 folate) dehydrogenase (D) and methenyl[H,I 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,Jfolate syn- thetase (S). Two crystal forms of the DC domain of the human cytosolic DCS enzyme have been grown from polyethyleneglycol solution. The monoclinic P2, crystals diffract to 2.8 A with a = 72.5 A, b = 68.5 A, c = 125.2 A, and p = 91.8" but were found to be twinned. The orthorhombic P2,2,2, crystals diffract to 2.5 A witha = 67.7 A, b = 135.9 A, c = 61.6 A, and contain two molecules per asymmetric unit. Proteins 26479-480