Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold.
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.
Scrutton
N S
NS
Department of Biochemistry, University of Leicester, University Road, Leicester LE1 7RH, UK.
Leys
D
D
D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D013763:Tetrahydrofolates / Q000378:metabolism*
D013763:Tetrahydrofolates; C030371:5,6,7,8-tetrahydrofolic acid; D000587:Oxidoreductases Acting on CH-NH Group Donors; C431689:dimethylglycine oxidase