Literature summary for 2.1.1.14 extracted from

Ubhi, D.; Robertus, J.
The cobalamin-independent methionine synthase enzyme captured in a substrate-induced closed conformation (2015), J. Mol. Biol., 427, 901-909 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Candida albicans

Organism

Organism	UniProt	Comment	Textmining
Candida albicans	P82610	-	-

Synonyms

Synonyms	Comment	Organism
Met6	-	Candida albicans

General Information

General Information	Comment	Organism
physiological function	substrate binding reorders the conformation of apo-Met6p to facilitate a direct SN2-type methylation reaction. The closed active site desolvates the active site save one water that serves as a conduit from His707 to protonate the tetrahydrofolate N5. Oscillations around the Zn cluster allow the thiolate to attack the methyl group and the protonated tetrahydrofolate is already activated as a reasonable leaving group. The transition state is likely to be a classic pyramidal structure with 3 methyl hydrogens in a plane and the incoming thiolate and departing tetrahydrofolate amine as axial ligands	Candida albicans

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Release 2023.1 (January 2023)