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Biochem Soc Trans. 2005 Aug;33(Pt 4):776-9.

Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold.

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1
Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, UK.

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.

PMID:
16042597
DOI:
10.1042/BST0330776
[Indexed for MEDLINE]
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