2.1.1.184: 23S rRNA (adenine2085-N6)-dimethyltransferase
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For detailed information about 23S rRNA (adenine2085-N6)-dimethyltransferase, go to the full flat file.
Word Map on EC 2.1.1.184
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2.1.1.184
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macrolide
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macrolide-lincosamide-streptogramin
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methyltransferases
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lincosamide
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unmethylated
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mtases
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streptogramine
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medicine
- 2.1.1.184
-
macrolide
-
macrolide-lincosamide-streptogramin
- methyltransferases
-
lincosamide
-
unmethylated
- mtases
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streptogramine
- medicine
Reaction
2 S-adenosyl-L-methionine + = 2 S-adenosyl-L-homocysteine +
Synonyms
23S ribosomal RNA adenine N-6 methyltransferase, EC 2.1.1.48, ErmC, ermC 23 S rRNA methyltransferase, ErmC 23S rRNA methyltransferase, ermC methylase, ErmC methyltransferase, ErmC', ErmC' methyltransferase, ErmC' MTase, erythromycin resistance protein, rRNA methyltransferase ErmC', rRNA:m6A methyltransferase ErmC'
ECTree
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Crystallization
Crystallization on EC 2.1.1.184 - 23S rRNA (adenine2085-N6)-dimethyltransferase
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crystallized by the hanging drop vapor diffusion method. Structure of the apo-enzyme at 2.2 A resolution. The crystal structures of ErmC' and of its complexes with the cofactor S-adenosyl-L-methionine, the reaction product S-adenosyl-L-homocysteine and the methyltransferase inhibitor sinefungin, respectively, show that the enzyme undergoes small conformational changes upon ligand binding
crystals of ErmC' are obtained by the hanging-drop vapor diffusion method. Crystal structure of ErmC' (a naturally occurring variant of ErmC) determined at 3.0 A resolution by multiple anomalous diffraction phasing methods. The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-L-methionine, followed by a smaller, alpha-helical RNA-recognition domain
the crystal structure of ErmC methyltransferase is used as a target for structure-based virtual screening of a database composed of 58679 lead-like compounds. Analysis of docking models of the identified inhibitors suggests a novel strategy to develop potent and clinically useful inhibitors