SAM-dependent methyltransferase

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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]]'>
<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]]'>
== Function ==
== 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)<ref>PMID:23180741</ref>.
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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>.
For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playground/CheR]].<ref>PMID:9628482</ref>.<br />
For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playground/CheR]].<ref>PMID:9628482</ref>.<br />
*SEE ALSO [[Chemotaxis protein]].
*SEE ALSO [[Chemotaxis protein]].
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== Structural highlights ==
== Structural highlights ==
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.
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.
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</StructureSection>
 
==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''<br />
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**[[4qvk]] – PaSDM – ''Podospora anserina''<br />
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**[[4ymg]] – PaSDM + SAM<br />
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**[[4ymh]] – PaSDM + SAH<br />
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**[[3ssm]], [[3sso]] – MgSDM + SAH – ''Micromonospora griseorubida''<br />
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**[[3ssn]] – MgSDM + SAH + mycinamin <br />
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*SAM-dependent N-methyltransferase
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**[[1vlm]] – TmSDM (mutant)
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*SAM-dependent C-methyltransferase
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**[[4m72]] – ShSDM – ''Streptomyces hygroscopicus''<br />
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**[[4m73]], [[4m74]] – ShSDM (mutant) <br />
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**[[4kib]] – ShSDM + SAH + methylphenylpyruvate <br />
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**[[4kic]] – ShSDM + SAM + phenylpyruvate <br />
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**[[4kif]], [[4kig]] – ShSDM + phenylpyruvate <br />
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**[[4m6x]], [[4m6y]], [[4m71]] – ShSDM (mutant) + SAH + methylphenylpyruvate <br />
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**[[5o4h]] – MmHCGC + SAM + pyridinol - ''Methanococcus maripaludis'' <br />
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**[[5o4n]], [[5o4j]], [[5o4m]] – MmHCGC + SAH + pyridinol <br />
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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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**[[3lga]] – PaSDM + SAH – ''Pyrococcus abyssi''<br />
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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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**[[5gm1]] – SbSDM + SAH – ''Streptomyces blastmyceticus''<br />
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**[[5gm2]] – SbSDM + SAH + teleocidin<br />
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**[[4x3q]] – SDM + SAH – ''Streptosporangium sibiricum''<br />
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**[[3h2b]] – CgSDM + pyrophosphate + SAH<br />
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**[[5bp7]] – SlSDM + SAH – ''Geobacter sulfurreducens''<br />
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**[[5epe]] – SDM + SAH –'' Thiobacillus denitrificans''<br />
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**[[5bp9]] – SDM + SAH – ''Bacterioides fragilis''<br />
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**[[2ybo]] – PsaSDM + SAH – ''Pseudomonas aeruginosa'' <br />
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**[[2ybq]] – PsaSDM + SAH + uroporphyrinogen <br />
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*Chemotaxis receptor methyltransferase (CheR)
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**[[1af7]] – StCheR – ''Salmonella typhimurium''<br />
 
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**[[1bc5]] – StCheR + chemotaxis receptor peptide
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[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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Michal Harel, Alexander Berchansky, Joel L. Sussman

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