23S rRNA (uridine2479-2'-O)-methyltransferase

23S rRNA (uridine2479-2'-O)-methyltransferase
Identifiers
EC number 2.1.1.208
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

23S rRNA (uridine2479-2'-O)-methyltransferase (EC 2.1.1.208, AviRb) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2479-2'-O)-methyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + uridine2479 in 23S rRNA S-adenosyl-L-homocysteine + 2'-O-methyluridine2479 in 23S rRNA

Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis.[4]

References

  1. Mosbacher, T.G.; Bechthold, A.; Schulz, G.E. (2005). "Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes". J. Mol. Biol. 345: 535–545. doi:10.1016/j.jmb.2004.10.051. PMID 15581897.
  2. Treede, I.; Jakobsen, L.; Kirpekar, F.; Vester, B.; Weitnauer, G.; Bechthold, A.; Douthwaite, S. (2003). "The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose". Mol. Microbiol. 49: 309–318. doi:10.1046/j.1365-2958.2003.03558.x. PMID 12828631.
  3. Weitnauer, G.; Gaisser, S.; Trefzer, A.; Stockert, S.; Westrich, L.; Quiros, L.M.; Mendez, C.; Salas, J.A.; Bechthold, A. (2001). "An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tu57". Antimicrob. Agents Chemother. 45: 690–695. doi:10.1128/aac.45.3.690-695.2001. PMC 90357. PMID 11181344.
  4. Krupkin, M.; Wekselman, I.; Matzov, D.; Eyal, Z.; Diskin Posner, Y.; Rozenberg, H.; Zimmerman, E.; Bashan, A.; Yonath, A. (2016). "Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding". Proc Natl Acad Sci U S A. 113 (44): E6796–E6805. doi:10.1073/pnas.1614297113. PMC 5098648. PMID 27791159.
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