2.1.1.230: 23S rRNA (adenosine1067-2'-O)-methyltransferase
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For detailed information about 23S rRNA (adenosine1067-2'-O)-methyltransferase, go to the full flat file.
Reaction
Synonyms
EC 2.1.1.66, NHR, NHR protein, nosiheptide resistance methyltransferase, nosiheptide-resistance methyltransferase, thiostrepton resistance methyltransferase, thiostrepton-resistance methylase, thiostrepton-resistance methyltransferase, TSR
ECTree
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General Information on EC 2.1.1.230 - 23S rRNA (adenosine1067-2'-O)-methyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
in the absence of the N-terminal domain, Tsr is catalytically inactive despite possessing the intact S-adenosyl-L-methionine binding sites and catalytic center. The Tsr-C-terminal domain dimer binds the RNA 30fold more weakly than the wild-type enzyme and is unable to promote the N-terminal domain-dependent RNA conformational change
physiological function
additional information
physiological function
methylation at adenosine1067 in 23S rRNA is essential for resistance against nosiheptide, a sulfur peptide antibiotic, which is produced by the nosiheptide-producing strain, Streptomyces actuosus
physiological function
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Streptomyces azureus is the producer of the peptide antibiotic thiostrepton. Thiostrepton inhibits protein synthesis by binding to the complex of 23S rRNA and protein L-11 which blocks processes associated with the GTP-hydrolysis center of the ribosome including the binding of guanine nucleotides, elongation factor proteins and tRNA. 23S rRNA (adenosine1067-2'-O)-methyltransferase confers resistance to thiostrepton
physiological function
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the enzyme is involved in resistance to thiostrepton
physiological function
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the methylase enzyme, responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton
physiological function
the nosiheptide producer Streptomyces actuosis prevents self-intoxication by expressing the enzyme, which methylates the 2'-hydroxyl of 23 S rRNA nucleotide adenosine 1067 within the antibiotic binding site. Methylation at A1067 blocks thiazole binding directly. This region of 23S rRNA is also the binding site for the ribosomal protein L11
physiological function
the thiostrepton producer Streptomyces azureus prevents self-intoxication by expressing the thiostrepton-resistance methyltransferase (Tsr), which methylates the 2'-hydroxyl of 23 S rRNA nucleotide adenosine 1067 within the thiostrepton binding site
additional information
each protomer of the homodimer containing an L30e-like amino-terminal domain and a SPOUT methyltransferase family catalytic carboxyl-terminal domain, both enzyme domains are required for high affinity RNA substrate binding. The Tsr-C-terminal domain has intrinsic, weak RNA affinity that is necessary to direct the specific high-affinity Tsr-RNA interaction via N-terminal domains, which have no detectable RNA affinity when isolated. The N-terminal domains increase RNA binding affinity and are necessary for catalysis, RNA binding mechanism, overview. The N-terminal domain of Tsr is an essential component of the RNA substrate recognition mechanism by both promoting high affinity RNA binding and activation of catalysis by the C-terminal domain
additional information
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each protomer of the homodimer containing an L30e-like amino-terminal domain and a SPOUT methyltransferase family catalytic carboxyl-terminal domain, both enzyme domains are required for high affinity RNA substrate binding. The Tsr-C-terminal domain has intrinsic, weak RNA affinity that is necessary to direct the specific high-affinity Tsr-RNA interaction via N-terminal domains, which have no detectable RNA affinity when isolated. The N-terminal domains increase RNA binding affinity and are necessary for catalysis, RNA binding mechanism, overview. The N-terminal domain of Tsr is an essential component of the RNA substrate recognition mechanism by both promoting high affinity RNA binding and activation of catalysis by the C-terminal domain
additional information
the NHR heterodimer requires only one functional subunit for RNA recognition and enzymatic activity. The catalytic residue is Arg135
additional information
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the NHR heterodimer requires only one functional subunit for RNA recognition and enzymatic activity. The catalytic residue is Arg135
