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Literature summary for 2.1.1.192 extracted from

  • Boal, A.K.; Grove, T.L.; McLaughlin, M.I.; Yennawar, N.H.; Booker, S.J.; Rosenzweig, A.C.
    Structural basis for methyl transfer by a radical SAM enzyme (2011), Science, 332, 1089-1092 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.192

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 [2Fe-2S] ferredoxin Escherichia coli
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 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine37 in tRNA + 2 reduced [2Fe-2S] ferredoxin Escherichia coli
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 2 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine37 in tRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P36979
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine37 in tRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Escherichia coli 2 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine37 in tRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?

Synonyms

Synonyms Comment Organism
RlmN
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
reduced [2Fe-2S] ferredoxin
-
 Escherichia coli
S-adenosyl-L-methionine SAM, crystal structures of RlmN and RlmN with SAM show that a single molecule of SAM coordinates the [4Fe-4S] cluster. Residue Cys 355 is S-methylated and located proximal to the SAM methyl group, suggesting that SAM involved in the initial methyl transfer binds at the same site Escherichia coli
[4Fe-4S] cluster a single molecule of SAM coordinates the [4Fe-4S] cluster Escherichia coli

General Information

General Information Comment Organism
evolution RlmN and Cfr belong to the radical SAM (RS) superfamily of enzymes. RlmN is proposed to be an evolutionary precursor to Cfr. The catalytic residues in theactive site are strictly conserved as are most of the surrounding residues within the core of the barrel Escherichia coli
additional information structure modelling and structure-function analysis of RlmN compared to Cfr from Staphylococcus aureus (EC 2.1.1.224), Escherichia coli RlmN and Staphylococcus aureus Cfr are mapped onto the RlmN structure, detailed overview. The RlmN reactions proceed by a ping-pong mechanism. The methyl group from one SAM molecule is initially appended to a conserved Cys355 in RlmN by a typical SN2 displacement. This SAM-derived one-carbon unit is then attached to the RNA by radical addition initiated by a 5'-deoxyadenosyl 5'-radical formed from a second molecule of SAM. Finally, this covalent intermediate is resolved by formation of a disulfide bond between the methyl-carrying Cys (mCys) residue and a second conserved Cys118. Nature and location of the rRNA binding site. The electrostatic surface potential for RlmN suggests the substrate may approach the active site from the bottom of the barrel. This extensive surface involves the core barrel, its extensions, and the extra domain, implicating the accessory elements in substrate interaction Escherichia coli
physiological function methyl transfer is essential in the synthesis of cellular metabolites and clinically relevant natural products, and in the modification of RNA, DNA, lipids, and proteins. Enzymes RlmN and Cfr catalyze methylation of a 23S rRNA nucleotide (adenosine 2503, A2503) ultimately located within the peptidyltransferase center of the 50S subunit of the bacterial ribosome near the entrance to the nascent peptide exit tunnel. RlmN methylates the C2 position of A2503, a housekeeping modification important in translational fidelity and the nascent peptide response. The radical SAM (RS) enzymes RlmN and Cfr methylate 23S ribosomal RNA, modifying the C2 or C8 position of adenosine 2503. The methyl groups are installed by a two-step sequence involving initial methylation of a conserved Cys residue (RlmN Cys 355) by SAM. Methyl transfer to the substrate requires reductive cleavage of a second equivalent of SAM. RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site Escherichia coli