CATH Classification

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 4JC0
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases.
Forouhar, F., Arragain, S., Atta, M., Gambarelli, S., Mouesca, J.M., Hussain, M., Xiao, R., Kieffer-Jaquinod, S., Seetharaman, J., Acton, T.B., Montelione, G.T., Mulliez, E., Hunt, J.F., Fontecave, M.
Nat.Chem.Biol.