Methionine adenosyltransferase

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spinqualitylabelsall models Monomer of the dimeric rat S-adenosylmethionine synthetase complex with methionine, phosphate, ATP (stick model), Mg+2 (green) and K+ (purple) ions (PDB entry 1o9t) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function S-adenosylmethionine synthetase (MAT) catalyzes the conversion of methionine and ATP to S-adenosylmethionine (AdoMet), pyrophosphate (PPi) and orthophosphate (Pi). AdoMet is a methyl donor. The catalytic entity of MAT is a dimer. MAT cofactors are Mg+2 (or Co+2) and K+ ions. Structural highlights The active site of MAT is located at the dimer interface[1].

3D structures of S-adenosylmethionine synthetase

22-August-2016

References

1. ↑ Gonzalez B, Pajares MA, Hermoso JA, Guillerm D, Guillerm G, Sanz-Aparicio J. Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism. J Mol Biol. 2003 Aug 8;331(2):407-16. PMID:12888348