Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold. (1st August 2005)

• Record Type: Journal Article
• Authors: Scrutton, N.S.; Leys, D.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 4(2005)
• Page Start: 776
• Page End: 779
• Publication Date: 2005-08-01
• Subjects: dimethylglycine dehydrogenase -- dimethylglycine oxidase -- folinic acid -- prototype -- pterin -- tetrahydrofolate; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0330776
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : The crystal structure of DMGO (dimethylglycine oxidase) from Arthrobacter globiformis in complex with folate compounds has revealed a novel THF (tetrahydrofolate)-binding fold [Leys, Basran and Scrutton (2003) EMBO J. 22, 4038–4048]. This fold is widespread among folate-binding proteins. The crystal structures of aminomethyltransferase (T-protein), YgfZ and TrmE all reveal similar THF-binding folds despite little similarity in sequence or function. The THF-binding site is highly specific for reduced folate compounds and most members of this fold family enhance the nucleophilic character of the THF N10 position.