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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 Function SAM-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)[1]. For Chemotaxis receptor methyltransferase CheR see details in [[Molecular Playgroun]d/CheR]].[2]. 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[3].

3D structures of SAM-dependent methyltrasferase

Updated on 23-August-2016

spinqualitylabelsall models Chemotaxis receptor methyltransferase CheR complex with S-adenosyl-L-homocysteine, 1af7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image For Chemotaxis receptor methyltransferase CheR see details in Molecular Playground/CheR.[4] of Chemotaxis receptor methyltransferase CheR (1af7).[5] SEE ALSO Chemotaxis protein.

References

1. ↑ Struck AW, Thompson ML, Wong LS, Micklefield J. S-adenosyl-methionine-dependent methyltransferases: highly versatile enzymes in biocatalysis, biosynthesis and other biotechnological applications. Chembiochem. 2012 Dec 21;13(18):2642-55. doi: 10.1002/cbic.201200556. Epub 2012, Nov 23. PMID:23180741 doi:http://dx.doi.org/10.1002/cbic.201200556
2. ↑ Djordjevic S, Stock AM. Chemotaxis receptor recognition by protein methyltransferase CheR. Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482
3. ↑ Lee JH, Bae B, Kuemin M, Circello BT, Metcalf WW, Nair SK, van der Donk WA. Characterization and structure of DhpI, a phosphonate O-methyltransferase involved in dehydrophos biosynthesis. Proc Natl Acad Sci U S A. 2010 Oct 12;107(41):17557-62. Epub 2010 Sep 27. PMID:20876132 doi:10.1073/pnas.1006848107
4. ↑ Djordjevic S, Stock AM. Chemotaxis receptor recognition by protein methyltransferase CheR. Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482
5. ↑ Djordjevic S, Stock AM. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Structure. 1997 Apr 15;5(4):545-58. PMID:9115443