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.
Conference Article| August 01 2005
Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold
- Views Icon Views
- Share Icon Share
N.S. Scrutton, D. Leys; Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold. Biochem Soc Trans 1 August 2005; 33 (4): 776–779. doi: https://doi.org/10.1042/BST0330776
Download citation file: