Cobalamin-independent methionine synthase, MetE, catalyses the synthesis of the amino acid methionine by the transfer of a methyl group from methyltetrahydrofolate to homocysteine [1]. The N-terminal and C-terminal domains of MetE together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilise a loop from the C-terminal domain.
Ferrer JL, Ravanel S, Robert M, Dumas R.
Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate.
J. Biol. Chem. 279 44235-8 2004
[PubMed: 15326182] http://dx.doi.org/10.1074/jbc.C400325200
Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML.
Metal active site elasticity linked to activation of homocysteine in methionine synthases.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 3286-91
[PubMed: 18296644] http://dx.doi.org/10.1073/pnas.0709960105