SAM-dependent methyltransferase

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{{STRUCTURE_3h2b| PDB=3h2b | SIZE=400| SCENE= |right|CAPTION=SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and pyrophosphate, [[3h2b]] }}
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<StructureSection load='' size='350' side='right' scene='51/510230/Cv/3' caption='SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and sulfate [[3ou6]]'>
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== Function ==
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'''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). The core of the SDM fold contains alternating β strands and α helices. See also [[Molecular Playground/CheR]].
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'''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''')<ref>PMID:23180741</ref>.
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For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playground/CheR]].<ref>PMID:9628482</ref>.<br />
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*SEE ALSO [[Chemotaxis protein]].
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== Structural highlights ==
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The <scene name='51/510230/Cv/5'>core of the SDM fold contains alternating β strands and α helices</scene>. SDM <scene name='51/510230/Cv/6'>active site is located between the 2 monomers</scene><ref>PMID:20876132</ref>. Water molecules are shown as red spheres.
==3D structures of SAM-dependent methyltrasferase==
==3D structures of SAM-dependent methyltrasferase==
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[[SAM-dependent methyltrasferase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*SAM-dependent O-methyltransferase
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**[[1o54]] – TmSDM – ''Thermotoga maritima''<br />
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**[[2hnk]] – SDM – ''Leptospira interrogans''<br />
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**[[3r3h]] – SDM – ''Legionella pneumophila''
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*SAM-dependent N-methyltransferase
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**[[1vlm]] – TmSDM (mutant)
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*SAM-dependent methyltransferase
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**[[1wzn]] – SDM – ''Pyrococcus horikoshii''<br />
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**[[2igt]] – SDM –'' Agrobacterium tumefaciens''<br />
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**[[3cgg]] – CgSDM – ''Corynebacterium glutamicum''<br />
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**[[3d2l]] - SDM – ''Exiguobacterium sibiricum''<br />
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**[[3dh0]] - SDM – ''Aquifex aeolicus''<br />
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**[[3dp7]] - SDM – ''Bacterioides vulgatus''<br />
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**[[3ggd]] - SDM – ''Anabaena variabilis''<br />
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**[[3sm3]] - SDM (mutant) – ''Methanosarcina mazei''<br />
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**[[3bkx]] – SDM – ''Lactobacillus casei''<br />
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**[[3kr9]] – SpSDM – ''Streptococcus pneumonia''<br />
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*SAM-dependent methyltransferase complex with SAM/SAH
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**[[3ku1]] – SpSDM + SAM<br />
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== References ==
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**[[3lga]] – PaSDM + SAH – ''Pyrococcus abyssi''<br />
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<references/>
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**[[3mb5]] – PaSDM + SAM<br />
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**[[3ou2]] – SlSDM + SAH – ''Streptomyces luridus''<br />
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**[[3ou6]] – SlSDM + SAM<br />
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**[[3ou7]] – SlSDM + SAM + phosphonic acid derivative<br />
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**[[3h2b]] – CgSDM + pyrophosphate + SAH<br />
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**[[5bp7]] – SlSDM + SAH – ''Geobacter sulfurreducens''<br />
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}}
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[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and sulfate 3ou6

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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

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