SAM-dependent methyltransferase
From Proteopedia
Line 1: | Line 1: | ||
{{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]] }} | ||
- | '''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. | + | '''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]]. |
==3D structures of SAM-dependent methyltrasferase== | ==3D structures of SAM-dependent methyltrasferase== | ||
+ | |||
+ | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
===SAM-dependent O-methyltransferase=== | ===SAM-dependent O-methyltransferase=== | ||
Line 25: | Line 27: | ||
[[3ggd]] - SDM – ''Anabaena variabilis''<br /> | [[3ggd]] - SDM – ''Anabaena variabilis''<br /> | ||
[[3sm3]] - SDM (mutant) – ''Methanosarcina mazei''<br /> | [[3sm3]] - SDM (mutant) – ''Methanosarcina mazei''<br /> | ||
- | [[3h2b]] – CgSDM + pyrophosphate + SAH | + | [[3h2b]] – CgSDM + pyrophosphate + SAH<br /> |
+ | [[1bc5]] – SDM + chemotaxis receptor peptide + SAH - ''Salmonella typhimurium'' | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 12:00, 4 April 2013
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.
Contents |
3D structures of SAM-dependent methyltrasferase
Updated on 04-April-2013
SAM-dependent O-methyltransferase
1o54 – TmSDM – Thermotoga maritima
2hnk – SDM – Leptospira interrogans
3r3h – SDM – Legionella pneumophila
SAM-dependent N-methyltransferase
1vlm – TmSDM (mutant)
SAM-dependent methyltransferase
1wzn – SDM – Pyrococcus horikoshii
2igt – SDM – Agrobacterium tumefaciens
3cgg – CgSDM – Corynebacterium glutamicum
3d2l - SDM – Exiguobacterium sibiricum
3dh0 - SDM – Aquifex aeolicus
3dp7 - SDM – Bacterioides vulgatus
3ggd - SDM – Anabaena variabilis
3sm3 - SDM (mutant) – Methanosarcina mazei
3h2b – CgSDM + pyrophosphate + SAH
1bc5 – SDM + chemotaxis receptor peptide + SAH - Salmonella typhimurium