Methionine synthase: Difference between revisions
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<StructureSection load='1k7y' size='310' side='right' caption='B-12 dependent fragment of E. coli methionine synthase with Cobalamin (in pink)' scene=''> | |||
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PDB ID: 1K7Y | PDB ID: 1K7Y | ||
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Revision as of 19:33, 2 April 2022
Methionine synthaseMethionine synthase
This page is being worked on during the Spring 2022 semester. Methionine is an essential amino acid required in order for our bodies to have healthy cell and tissue growth. Unfortunately, it is not naturally derived and dependent on our diets. Methionine synthase methylates homocysteine, another amino acid obtained typically by any meat we consume, to methionine[1].
EC: 2.1.1.13 PDB ID: 1K7Y
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The change from homocysteine to methionine is one methyl group on N-5 donated from methyltetrahydrofolate (MTHF), a product of Methylenetetrahydrofolate reductase (MTHFR), with a protein-bound B-12 vitamin Cobalamin as the methyl carrier.
Vitamin B-12Vitamin B-12
Oxidation States of CobalaminOxidation States of Cobalamin
RelevanceRelevance
Structural highlightsStructural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
ReferencesReferences
- ↑ Kung Y, Ando N, Doukov TI, Blasiak LC, Bender G, Seravalli J, Ragsdale SW, Drennan CL. Visualizing molecular juggling within a B(12)-dependent methyltransferase complex. Nature. 2012 Mar 14. doi: 10.1038/nature10916. PMID:22419154 doi:10.1038/nature10916
- ↑ Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML. Domain alternation switches B(12)-dependent methionine synthase to the activation conformation. Nat Struct Biol. 2002 Jan;9(1):53-6. PMID:11731805 doi:10.1038/nsb738