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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]] }}
{{STRUCTURE_3h2b| PDB=3h2b | SIZE=400| SCENE= |right|CAPTION=SAM-dependent methyltransferase dimer complex with S-adenosyl-L-homocysteine and pyrophosphate, [[3h2b]] }}
== 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>. See also [[Molecular Playground/CheR]].
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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>.
 +
<StructureSection load='1af7' size='350' side='right' scene='47/479962/Cv/1' caption='Chemotaxis receptor methyltransferase CheR complex with S-adenosyl-L-homocysteine, [[1af7]]'>
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For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playgroun]d/CheR]].<ref>PMID:9628482</ref>
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*<scene name='47/479962/Cv/2'>S-adenosyl-L-homocysteine binding site</scene> of Chemotaxis receptor methyltransferase CheR ([[1af7]]).<ref>PMID:9115443</ref>
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*SEE ALSO [[Chemotaxis protein]].
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</StructureSection>
== Structural highlights ==
== Structural highlights ==
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**[[3h2b]] – CgSDM + pyrophosphate + SAH<br />
**[[3h2b]] – CgSDM + pyrophosphate + SAH<br />
**[[5bp7]] – SlSDM + SAH – ''Geobacter sulfurreducens''<br />
**[[5bp7]] – SlSDM + SAH – ''Geobacter sulfurreducens''<br />
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 +
<StructureSection load='1af7' size='350' side='right' scene='47/479962/Cv/1' caption='Chemotaxis receptor methyltransferase CheR complex with S-adenosyl-L-homocysteine, [[1af7]]'>
 +
 +
For '''Chemotaxis receptor methyltransferase CheR''' see details in [[Molecular Playground/CheR]].<ref>PMID:9628482</ref>
 +
*<scene name='47/479962/Cv/2'>S-adenosyl-L-homocysteine binding site</scene> of Chemotaxis receptor methyltransferase CheR ([[1af7]]).<ref>PMID:9115443</ref>
 +
*SEE ALSO [[Chemotaxis protein]].
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</StructureSection>
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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
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 07:56, 23 August 2016

Template:STRUCTURE 3h2b

Contents

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].

Chemotaxis receptor methyltransferase CheR complex with S-adenosyl-L-homocysteine, 1af7

Drag the structure with the mouse to rotate

Structural highlights

The core of the SDM fold contains alternating β strands and α helices.

3D structures of SAM-dependent methyltrasferase

Updated on 23-August-2016

Chemotaxis receptor methyltransferase CheR complex with S-adenosyl-L-homocysteine, 1af7

Drag the structure with the mouse to rotate

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. ↑ 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
  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

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