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 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.
Arragain, S., Garcia-Serres, R., Blondin, G., Douki, T., Clemancey, M., Latour, J.M., Forouhar, F., Neely, H., Montelione, G.T., Hunt, J.F., Mulliez, E., Fontecave, M., Atta, M.
J.Biol.Chem.