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Literature summary extracted from

  • Lebars, I.; Yoshizawa, S.; Stenholm, A.R.; Guittet, E.; Douthwaite, S.; Fourmy, D.
    Structure of 23S rRNA hairpin 35 and its interaction with the tylosin-resistance methyltransferase RlmAII (2003), EMBO J., 22, 183-192.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.188 expression in Escherichia coli Streptococcus pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.188 Streptococcus pneumoniae
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-
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.188
-
 Streptococcus pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.188 S-adenosyl-L-methionine + guanine748 in 23S rRNA the enzyme methylates 23S rRNA at nucleotide G748, which is situated in a stem-loop (hairpin 35) at the macrolide binding site of the ribosome. Binding of RlmAII methyltransferase induces chemical shift changes in the RNA. The conformation of hairpin 35 that interacts with RlmAII is radically different from the structure this hairpin adopts within the 50S subunit Streptococcus pneumoniae S-adenosyl-L-homocysteine + N1-methylguanine748 in 23S rRNA
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.188 methyltransferase RlmAII
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 Streptococcus pneumoniae
2.1.1.188 RlmAII
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 Streptococcus pneumoniae
2.1.1.188 TlrB
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 Streptococcus pneumoniae