SAM-dependent methyltransferase

spinqualitylabelsall models SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and sulfate 3ou6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function SAM-dependent methyltransferase or S-adenosylmethionine-dependent methyltransferase (SDM) utilizes the methyl donor S-adenosyl-L-methionine (SAM) as a cofactor to methylate proteins, small molecules, lipids and nucleic acids. SAM forms S-adenosyl-L-homocysteine (SAH) upon demethylation. About 120 members of the SDM family have been identified. They differ in their substrate specificity and the atom targeted for methylation (N, O, C, S). For Chemotaxis receptor methyltransferase CheR see details in Molecular Playground/CheR.. SEE ALSO Chemotaxis protein. Structural highlights The core of the SDM fold contains alternating β strands and α helices. SDM active site is located between the 2 monomers. Water molecules are shown as red spheres. 3D structures of SAM-dependent methyltrasferase SAM-dependent methyltrasferase 3D structures

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