AdoMet MTase
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| SAM-dependent MTases superfamily | |
|---|---|
| File:PDB 2igt EBI.jpg Cartoon representation of the molecular structure of the Crystal Structure of the SAM Dependent Methyltransferase from Agrobacterium tumefaciens (PDB: 2igt) | |
| Identifiers | |
| Symbol | SAM-dependent_MTases |
| ECOD | 2003.1.5 |
| InterPro | IPR029063 |
| AdoMet_MTase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | AdoMet_MTase | ||||||||
| Pfam | PF07757 | ||||||||
| Pfam clan | CL0063 | ||||||||
| InterPro | IPR011671 | ||||||||
| |||||||||
S-adenosylmethionine-dependent methyltransferase (SAM-MTase or AdoMet-MTase) is a conserved protein domain and protein superfamily.[1] SAM-MTase proteins are methyltransferases.[2] There are five protein families within SAM-MTase,
SAM-MTases use S-adenosyl-L-methionine as a substrate for methylation, creating the product S-adenosyl-L-homocysteine.[3]
Structure and subgroups
[edit | edit source]All SAM-MTases contain a structurally conserved SAM-binding domain consisting of a central seven-stranded beta-sheet that is flanked by three alpha-helices per side of the sheet.[4]
A review published in 2003 divides all methyltransferases into 5 main classes based on the structure of their catalytic domain (fold):[5]
- class I: Rossmann-like α/β, the largest subgroup.[3]
- class II: TIM β/α-barrel α/β
- class III: tetrapyrrole methylase α/β
- class IV: SPOUT α/β
- class V: SET domain all β
References
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