Methionine synthase

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This page is being worked on during the Spring 2022 semester.
This page is being worked on during the Spring 2022 semester.
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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 is dependent on our diet. Methionine synthase methylates homocysteine, another amino acid obtained typically by meat we consume, to methionine. The change from homocysteine to methionine is one methyl group, by which is received from methyltetrahydrofolate (MTHF), a product of Methylenetetrahydrofolate reductase (MTHFR), as the methyl donor and a protein-bound B-12 vitamin Cobalamin as the methyl carrier <ref>DOI: 10.1038/nature10916</ref>.
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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<ref>DOI: 10.1038/nature10916</ref>.
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The change from homocysteine to methionine is one methyl group, by which is received from methyltetrahydrofolate (MTHF), a product of Methylenetetrahydrofolate reductase (MTHFR), as the methyl donor and a protein-bound B-12 vitamin Cobalamin as the methyl carrier.
EC: 2.1.1.13
EC: 2.1.1.13
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PDB ID: 1K7Y
PDB ID: 1K7Y

Revision as of 15:17, 30 March 2022

Contents

Methionine synthase

B-12 dependent fragment of E. coli methionine synthase with Cobalamin (in pink)

Drag the structure with the mouse to rotate

Image:MetHsynthase.jpeg

Vitamin B-12

Oxidation States of Cobalamin

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Structural 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>

References

[2]

  1. ↑ 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
  2. ↑ 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

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Kia Yang, Karsten Theis, Michal Harel, Anna Postnikova, Michael O'Shaughnessy

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