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2.1.1.14: 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

This is an abbreviated version!
For detailed information about 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.14

Reaction

5-methyltetrahydropteroyltri-L-glutamate
+
L-homocysteine
=
tetrahydropteroyltri-L-glutamate
 +
L-methionine

Synonyms

5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase, AtMetE, cobalamin-independent methionine synthase, cobalamin-independent methionine synthase (MetE), homocysteine methylase, Met-8, MET1, Met6, Met6p, MetE, methionine synthase MetE, methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase, methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase, MS1, PpMetE, tetrahydropteroyltriglutamate methyltransferase, TM1286

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.14 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

Crystallization

Crystallization on EC 2.1.1.14 - 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallization with L-homocysteine or met and ternary complexes with folate substrates, sitting drop method
-
binding of L-homocysteine or methionine results in conformational rearrangements at the amino acid binding pocket, moving the catalytic zinc into position to activate the thiol group. Active-site residues Asn126 and Tyr660 play key roles in catalysis
ternary complex with both substrates bound in a closed form of the enzyme. The closing is described in terms of a hinge between the N- and C-terminal TIM barrels and a rearrangement of key loops within the C domain
structures of native MetE in complex with either Zn2+ or Cd2+, at resolution limits of 2.10 A and 1.88 A, respectively. The monomeric protein contains two domains, each containing a (betaalpha)8 barrel core, and a long alpha-helical segment spans the length of the protein, connecting the domains. Zn2+ bound in the C-terminal domain exhibits tetrahedral coordination with the side chains of His652, Cys654, Glu676 and Cys737
hanging drop vapour diffusion method
-
hanging-drop vapor diffusion method
an unusual-barrel structure in which the active site lies between the tops of the two (betaalpha)8 barrels
-
vapor batch (microbatch) method using 25% poly(ethylene glycol) 4000, 0.2 M ammonium sulfate, and 0.1 M sodium acetate (pH 4.6)