Methionine synthase: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<StructureSection load='<scene name='90/907471/Superposition_1/2'>initial scene</scene>' size='310' side='right' caption='N-terminal containing catalytic cycle with two domains: 5-me THF and Hcy. C-terminal containing reactivation cycle with two domains: Cobalamin and SAM' (PBD ID: 1k7y)' scene=''> | |||
=== Domain organization === | === Domain organization === | ||
Methionine synthase contains four domains, each with a unique function that bind to Cob(I)alamin as the methyl carrier. In the N-terminal, 5-me THF donates a methyl in the catalytic cycle to Cob(I)alamin, which then donates it to homocysteine to form methionine. However, every 2,000 cycles or so, Cob(I)alamin becomes oxidized (as shown below in the darker yellow color) and now requires reduction and remethylation triggering the reactivation cycle. In the C-terminal, S-adenosylmethionine or SAM donates methyl with Flavodoxin as the electron donor<ref name="Bandarian et al">DOI: 10.1038/nsb738</ref>. | Methionine synthase contains four domains, each with a unique function that bind to Cob(I)alamin as the methyl carrier. In the N-terminal, 5-me THF donates a methyl in the catalytic cycle to Cob(I)alamin, which then donates it to homocysteine to form methionine. However, every 2,000 cycles or so, Cob(I)alamin becomes oxidized (as shown below in the darker yellow color) and now requires reduction and remethylation triggering the reactivation cycle. In the C-terminal, S-adenosylmethionine or SAM donates methyl with Flavodoxin as the electron donor<ref name="Bandarian et al">DOI: 10.1038/nsb738</ref>. | ||
<scene name='90/907471/Superposition_1/2'>Text To Be Displayed</scene> | |||
[[Image:Methionine synthase domains.gif]] | [[Image:Methionine synthase domains.gif]] | ||
