Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.224
Description:23S rRNA (adenine(2503)-C(8))-methyltransferase.
Cath: 1.10.150.530; 3.20.20.70; 4.10.180.60;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.224
BRENDA Enzyme Link: BRENDA 2.1.1.224
KEGG Enzyme Link: KEGG2.1.1.224
BioCyc Enzyme Link: BioCyc 2.1.1.224
ExPASy Enzyme Link: ExPASy2.1.1.224
EC2PDB Enzyme Link: EC2PDB 2.1.1.224
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.224
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.224
IntEnz Enzyme Link: IntEnz 2.1.1.224
MEDLINE Enzyme Link: MEDLINE 2.1.1.224
MSA:

2.1.1.224;

Phylogenetic Tree:

2.1.1.224;

Uniprot:
M-CSA:
RHEA:42632 adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + 8-methyladenosine(2503) in 23S rRNA + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[S+;H0:8](-[*:9])-[CH2;+0:10]-[*:11].[*:12]-[S+;H0:13](-[*:14])-[CH3;+0:15].[*:16]:[cH;+0:17]:[*:18]>>[*:11]-[CH3;+0:10].[*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:12]-[S;H0;+0:13]-[*:14].[*:7]-[S;H0;+0:8]-[*:9].[*:16]:[c;H0;+0:17](:[*:18])-[CH3;+0:15]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN.Silakov A, Grove TL, Radle MI, Bauerle MR, Green MT, Rosenzweig AC, Boal AK, Booker SJ2014 Jun 1124806349
A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr.Grove TL, Livada J, Schwalm EL, Green MT, Booker SJ, Silakov A2013 Jul23644479
Covalent intermediate in the catalytic mechanism of the radical S-adenosyl-L-methionine methyl synthase RlmN trapped by mutagenesis.McCusker KP, Medzihradszky KF, Shiver AL, Nichols RJ, Yan F, Maltby DA, Gross CA, Fujimori DG2012 Oct 3123088750
Structural basis for methyl transfer by a radical SAM enzyme.Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC2011 May 2721527678
A radically different mechanism for S-adenosylmethionine-dependent methyltransferases.Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ2011 Apr 2921415317
RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift.Yan F, Fujimori DG2011 Mar 821368151
RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA.Yan F, LaMarre JM, Röhrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG2010 Mar 2420184321
Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria.Kaminska KH, Purta E, Hansen LH, Bujnicki JM, Vester B, Long KS2010 Mar20007606
Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria.Giessing AM, Jensen SS, Rasmussen A, Hansen LH, Gondela A, Long K, Vester B, Kirpekar F2009 Feb19144912