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Literature summary extracted from

  • 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.
    Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase (2010), J. Biol. Chem., 285, 5792-5801.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.4.4
-
Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.4.4 2.0 A crystal structure of the central radical S-adenosyl-L-methionine and the C-terminal tRNA methyltransferase 2 and MiaB domainsTRAM in apo-RimO. Although the core of the open TIM barrel of the radical S-adenosyl-L-methionine domain is conserved, RimO shows differences in domain organization compared with other radical S-adenosyl-L-methionine enzymes. The unusually acidicTRAM domain, likely to bind the basic S12 protein, is located at the distal edge of the radical AdoMet domain. The basic S12 protein substrate is likely to bind RimO through interactions with both the TRAM domain and the concave surface of the incomplete TIM barrel Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
2.8.4.4 Thermotoga maritima Q9X2H6
-
-
2.8.4.4 Thermotoga maritima DSM 3109 Q9X2H6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.4.4 3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
Thermotoga maritima 3,3-bismethylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
?
2.8.4.4 3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
Thermotoga maritima DSM 3109 3,3-bismethylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
?
2.8.4.4 Asp89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
Thermotoga maritima 3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
?
2.8.4.4 Asp89-[ribosomal protein S12 20mer peptide] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
-
Thermotoga maritima DSM 3109 3-methylthioaspartate89-[ribosomal protein S12 20mer peptide] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
-
?
2.8.4.4 additional information holo-RimO can specifically methylthiolate the aspartate residue of a 20mer peptide derived from S12, yielding a mixture of mono- and bismethylthio derivatives Thermotoga maritima ?
-
?
2.8.4.4 additional information holo-RimO can specifically methylthiolate the aspartate residue of a 20mer peptide derived from S12, yielding a mixture of mono- and bismethylthio derivatives Thermotoga maritima DSM 3109 ?
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.4.4 [4Fe-4S]-center enzyme contains two [4Fe-4S] centers, one presumably bound to three invariant cysteines in the central radical S-adenosylmethionine domain and the other to three invariant cysteines in the N-terminal UPF0004 domain Thermotoga maritima