2.1.1.184: 23S rRNA (adenine2085-N6)-dimethyltransferase

This is an abbreviated version!
For detailed information about 23S rRNA (adenine2085-N6)-dimethyltransferase, go to the full flat file.

Reaction

2 S-adenosyl-L-methionine +

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

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.184 23S rRNA (adenine2085-N6)-dimethyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
322	AA Sequence
3	Application
5	Cloned(Commentary)
3	Crystallization (Commentary)
2	Expression
3	General Information
3	IC50 Value
8	Inhibitors
48	kcat/KM [mM/s]
6	Ki Value [mM]
58	KM Value [mM]
1	Localization
6	Natural Substrates/ Products (Substrates)
17	Organism
1	PDB ID
6	pH Optimum
1	pH Range
35	Protein Variants
4	Purification (Commentary)
5	Reaction
15	Reference
24	Substrates and Products (Substrate)
20	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
49	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 2.1.1.184 - 23S rRNA (adenine2085-N6)-dimethyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Bacillus subtilis

P13956

705109

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

Bacillus subtilis

P13956

485441

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

Bacillus subtilis

P13956

703219