CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.50 | OB fold (Dihydrolipoamide Acetyltransferase, E2P) |
|
2.40.50.140 | Nucleic acid-binding proteins |
Domain Context
CATH Clusters
| Superfamily | Nucleic acid-binding proteins |
| Functional Family | Ribosomal protein S12 methylthiotransferase RimO |
Enzyme Information
| 2.8.4.4 |
[Ribosomal protein S12] (aspartate(89)-C(3))-methylthiotransferase.
based on mapping to UniProt Q9X2H6
L-aspartate-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine.
-!- This bacterial enzyme binds two [4Fe-4S] clusters. -!- A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters. -!- In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge. -!- In the second reaction the enzyme catalyzes the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylsulfanyl group to aspartate(89) (Escherichia coli numbering). -!- The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes.
|
UniProtKB Entries (1)
| Q9X2H6 |
RIMO_THEMA
Thermotoga maritima MSB8
Ribosomal protein S12 methylthiotransferase RimO
|
PDB Structure
| PDB | 2QGQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Post-translational Modification of Ribosomal Proteins: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF RimO FROM THERMOTOGA MARITIMA, A RADICAL S-ADENOSYLMETHIONINE METHYLTHIOTRANSFERASE.
J.Biol.Chem.
|
