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Literature summary extracted from

  • Challand, M.R.; Salvadori, E.; Driesener, R.C.; Kay, C.W.; Roach, P.L.; Spencer, J.
    Cysteine methylation controls radical generation in the Cfr radical AdoMet rRNA methyltransferase (2013), PLoS ONE, 8, e67979.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.192 expressed in Escherichia coli Rosetta2(DE3)pLysS cells Mammaliicoccus sciuri
2.1.1.224 expressed in Escherichia coli Rosetta2(DE3)pLysS cells Mammaliicoccus sciuri
2.1.1.224 gene cfr, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain +Rosetta2(DE3) Staphylococcus aureus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.192 C338A the mutant binds S-adenosyl-L-methionine with wild type affinity, while oxidation of the [4Fe-4S] cluster is not observed Mammaliicoccus sciuri
2.1.1.224 C338A the mutant binds S-adenosyl-L-methionine with wild type affinity, while oxidation of the [4Fe-4S] cluster is not observed Mammaliicoccus sciuri
2.1.1.224 C338A site-directed mutagenesis, Cys338Ala Cfr binds S-adenosyl-L-methionine with equivalent affinity, oxidation of the [4Fe-4S] cluster is not observed Staphylococcus aureus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.192 41085
-
 x * 41085, electrospray mass spectrometry Mammaliicoccus sciuri
2.1.1.192 41088
-
 x * 41088, fully methylated protein, calculated from amino acid sequence Mammaliicoccus sciuri
2.1.1.224 41085
-
 x * 41085, electrospray mass spectrometry Mammaliicoccus sciuri
2.1.1.224 41088
-
 x * 41088, fully methylated protein, calculated from amino acid sequence Mammaliicoccus sciuri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.192 S-adenosyl-L-methionine + adenine2503 in 23S rRNA Mammaliicoccus sciuri
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
-
 ?
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin Staphylococcus aureus
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2.1.1.224 additional information Staphylococcus aureus enzyme Cfr methylates adenosine 2503 of the 23S rRNA in the peptidyltransferase centre (P-site) of the bacterial ribosome. In wild-type Cfr, where Cys338 is methylated, S-adenosyl-L-methionine binding leads to rapid oxidation of the [4Fe-4S] cluster and production of 5'-deoxyadenosine ?
-
 ?
2.1.1.224 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin Mammaliicoccus sciuri
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + oxidized [2Fe-2S] ferredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.192 Mammaliicoccus sciuri Q9FBG4
-
-
2.1.1.224 Mammaliicoccus sciuri Q9FBG4
-
-
2.1.1.224 Staphylococcus aureus
-
 methicillin-resistant, gene cfr
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin enzyme Cfr consumes two AdoMet equivalents per reaction cycle to support both methyl transfer to Cfr Cys338 (AdoMet1, step 1) and subsequently generation of the 59dA. radical (AdoMet2, step2) Staphylococcus aureus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.192 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
-
 Mammaliicoccus sciuri S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
-
 ?
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
-
 Staphylococcus aureus S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin enzyme Cfr consumes two AdoMet equivalents per reaction cycle to support both methyl transfer to Cfr Cys338 (AdoMet1, step 1) and subsequently generation of the 59dA. radical (AdoMet2, step2) Staphylococcus aureus S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2.1.1.224 additional information enzyme Cfr methylates adenosine 2503 of the 23S rRNA in the peptidyltransferase centre (P-site) of the bacterial ribosome. In wild-type Cfr, where Cys338 is methylated, S-adenosyl-L-methionine binding leads to rapid oxidation of the [4Fe-4S] cluster and production of 5'-deoxyadenosine Staphylococcus aureus ?
-
 ?
2.1.1.224 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin
-
 Mammaliicoccus sciuri S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + oxidized [2Fe-2S] ferredoxin
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.192 ? x * 41085, electrospray mass spectrometry Mammaliicoccus sciuri
2.1.1.192 ? x * 41088, fully methylated protein, calculated from amino acid sequence Mammaliicoccus sciuri
2.1.1.224 ? x * 41085, electrospray mass spectrometry Mammaliicoccus sciuri
2.1.1.224 ? x * 41088, fully methylated protein, calculated from amino acid sequence Mammaliicoccus sciuri

Synonyms

EC Number Synonyms Comment Organism
2.1.1.192 Cfr
-
 Mammaliicoccus sciuri
2.1.1.192 radical AdoMet rRNA methyltransferase
-
 Mammaliicoccus sciuri
2.1.1.224 Cfr
-
 Staphylococcus aureus
2.1.1.224 Cfr
-
 Mammaliicoccus sciuri
2.1.1.224 radical AdoMet rRNA methyltransferase
-
 Mammaliicoccus sciuri

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.192 [4Fe-4S]-center the enzyme contains a [4Fe-4S] cluster Mammaliicoccus sciuri
2.1.1.224 Ferredoxin enzyme Cfr contains a single [4Fe-4S] cluster that binds two separate molecules of S-adenosyl-L-methionine during the reaction cycle Staphylococcus aureus
2.1.1.224 S-adenosyl-L-methionine enzyme Cfr contains a single [4Fe-4S] cluster that binds two separate molecules of S-adenosyl-L-methionine during the reaction cycle Staphylococcus aureus
2.1.1.224 [4Fe-4S]-center the enzyme contains a [4Fe-4S] cluster Mammaliicoccus sciuri

General Information

EC Number General Information Comment Organism
2.1.1.224 additional information the presence of a methyl group on Cfr Cys338 is a key determinant of the activity of the enzyme towards S-adenosyl-L-methionine, thus enabling a single active site to support two distinct modes of S-adenosyl-L-methionine cleavage Staphylococcus aureus
2.1.1.224 physiological function enzyme Cfr methylates adenosine 2503 of the 23S rRNA in the peptidyltransferase centre (P-site) of the bacterial ribosome. This modification protects host bacteria, notably methicillin-resistant Staphylococcus aureus (MRSA), from numerous antibiotics, including agents (e.g. linezolid, retapamulin) Staphylococcus aureus