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Literature summary for 2.1.1.188 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)

Cloned (Comment) Organism
expression in Escherichia coli Streptococcus pneumoniae

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
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Purification (Commentary)

Purification (Comment) Organism
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Streptococcus pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms Comment Organism
methyltransferase RlmAII
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Streptococcus pneumoniae
RlmAII
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Streptococcus pneumoniae
TlrB
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Streptococcus pneumoniae