Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.230
Description:23S rRNA (adenosine(1067)-2'-O)-methyltransferase.
Alternative Name: Thiostrepton-resistance methylase.
Nosiheptide-resistance methyltransferase.
23S rRNA A(1067) 2'-methyltransferase.
Cath: 3.30.1330.30; 3.40.1280.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.230
BRENDA Enzyme Link: BRENDA 2.1.1.230
KEGG Enzyme Link: KEGG2.1.1.230
BioCyc Enzyme Link: BioCyc 2.1.1.230
ExPASy Enzyme Link: ExPASy2.1.1.230
EC2PDB Enzyme Link: EC2PDB 2.1.1.230
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.230
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.230
IntEnz Enzyme Link: IntEnz 2.1.1.230
MEDLINE Enzyme Link: MEDLINE 2.1.1.230
MSA:

2.1.1.230;

Phylogenetic Tree:

2.1.1.230;

Uniprot:
M-CSA:
RHEA:43212 adenosine(1067) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methyladenosine(1067) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2'-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA.Bechthold A, Floss HG1994 Sep 17925357
Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton.Thompson J, Schmidt F, Cundliffe E1982 Jul 256806287
Crystal structure of the nosiheptide-resistance methyltransferase of Streptomyces actuosus.Yang H, Wang Z, Shen Y, Wang P, Jia X, Zhao L, Zhou P, Gong R, Li Z, Yang Y, Chen D, Murchie AI, Xu Y2010 Aug 320550164