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  Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin

Schlünzen, F., Pyetan, E., Fucini, P., Yonath, A., & Harms, J. M. (2004). Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin. Molecular Microbiology, 54(5), 1287-1294. doi:10.1111/j.1365-2958.2004.04346.x.

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Genre: Zeitschriftenartikel
Alternativer Titel : Mol Microbiol

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 Urheber:
Schlünzen, Frank1, Autor
Pyetan, Erez, Autor
Fucini, Paola2, Autor           
Yonath, Ada, Autor
Harms, Jörg M., Autor
Affiliations:
1Max Planck Society, ou_persistent13              
2Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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 Zusammenfassung: Tiamulin, a prominent member of the pleuromutilin class of antibiotics, is a potent inhibitor of protein synthesis in bacteria. Up to now the effect of pleuromutilins on the ribosome has not been determined on a molecular level. The 3.5 Å structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin provides for the first time a detailed picture of its interactions with the 23S rRNA, thus explaining the molecular mechanism of the antimicrobial activity of the pleuromutilin class of antibiotics. Our results show that tiamulin is located within the peptidyl transferase center (PTC) of the 50S ribosomal subunit with its tricyclic mutilin core positioned in a tight pocket at the A-tRNA binding site. Also, the extension, which protrudes from its mutilin core, partially overlaps with the P-tRNA binding site. Thereby, tiamulin directly inhibits peptide bond formation. Comparison of the tiamulin binding site with other PTC targeting drugs, like chloramphenicol, clindamycin and streptogramins, may facilitate the design of modified or hybridized drugs that extend the applicability of this class of antibiotics.

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Sprache(n): eng - English
 Datum: 2004-12
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: -
 Identifikatoren: eDoc: 225156
DOI: 10.1111/j.1365-2958.2004.04346.x
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Titel: Molecular Microbiology
  Alternativer Titel : Mol Microbiol
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 54 (5) Artikelnummer: - Start- / Endseite: 1287 - 1294 Identifikator: ISSN: 0950-382X