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Cobalamin-independent methionine synthase catalyzes the transfer of a methyl group from methyltetrahydrofolate to L-homocysteine without making use of an intermediate methyl service provider. Crystallographic evaluations of MetE from T. maritima reveal unusual dual-barrel framework in which the active site lies in between the tops of both 8 barrels. The zinc-binding site in MetE is identified from the 3Zn site in the relevant enzymes, MetH and betaine-- homocysteine methyltransferase, by its setting in the barrel and by the metal ligands, which are histidine, cysteine, glutamate, and cysteine in the resting form of MetE. The folate substrate is not totally related to the N-terminal barrel; rather, components from both barrels add binding factors in a binary facility in which the folate substrate is improperly oriented for methyl transfer.
Source link: https://www.osti.gov/biblio/1627135
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