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Literature summary for 2.1.1.224 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
Search for more literature for 2.1.1.224

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
C338A the mutant binds S-adenosyl-L-methionine with wild type affinity, while oxidation of the [4Fe-4S] cluster is not observed Mammaliicoccus sciuri
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]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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 ?
-
 ?
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

Organism UniProt Comment Textmining
Mammaliicoccus sciuri Q9FBG4
-
-
Staphylococcus aureus
-
 methicillin-resistant, gene cfr
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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
-
 ?
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 ?
-
 ?
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

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

Synonyms

Synonyms Comment Organism
Cfr
-
 Staphylococcus aureus
Cfr
-
 Mammaliicoccus sciuri
radical AdoMet rRNA methyltransferase
-
 Mammaliicoccus sciuri

Cofactor

Cofactor Comment Organism Structure
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
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
[4Fe-4S]-center the enzyme contains a [4Fe-4S] cluster Mammaliicoccus sciuri

General Information

General Information Comment Organism
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
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