Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A.
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Autor
Kaminishi, TatsuyaSchedlbauer, Andreas
Fabbretti, Attilio
Brandi, Letizia
Ochoa Lizarralde, Borja
He, Cheng-Guang
Milon, Pohl
Connell, Sean R
Gualerzi, Claudio O
Fucini, Paola
Fecha de publicación
2015-11-16Palabras clave
Binding SitesCinnamates
X-Ray Crystallography
Hygromycin B
Models Molecular
Peptidyl Transferases
Ribosome Subunits
RNA
MeSH
Binding SitesCinnamates
Crystallography, X-Ray
Hygromycin B
Models, Molecular
Peptidyl Transferases
Protein Synthesis Inhibitors
RNA, Transfer, Amino Acyl
Ribosome Subunits, Large, Bacterial
xmlui.metadata.dc.contributor.email
[email protected]
Metadatos
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Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A. 2015, 43 (20):10015-25 Nucleic Acids Res.Editorial
Oxford University PressJournal
Nucleic acids research (Nucleic Acids Res.)DOI
10.1093/nar/gkv975PubMed ID
26464437Enlaces adicionales
http://nar.oxfordjournals.org/content/43/20/10015.longResumen
Hygromycin A (HygA) binds to the large ribosomal subunit and inhibits its peptidyl transferase (PT) activity. The presented structural and biochemical data indicate that HygA does not interfere with the initial binding of aminoacyl-tRNA to the A site, but prevents its subsequent adjustment such that it fails to act as a substrate in the PT reaction. Structurally we demonstrate that HygA binds within the peptidyl transferase center (PTC) and induces a unique conformation. Specifically in its ribosomal binding site HygA would overlap and clash with aminoacyl-A76 ribose moiety and, therefore, its primary mode of action involves sterically restricting access of the incoming aminoacyl-tRNA to the PTC.Tipo
info:eu-repo/semantics/articleDerechos
info:eu-repo/semantics/openAccessIdioma
engISSN
1362-4962Patrocinadores
Bizkaia:Talent and the European Union's Seventh Framework Program (Marie Curie Actions; COFUND; to S.C., A.S., T.K.); Marie Curie Actions Career Integration Grant (PCIG14-GA-2013-632072 to P.F.); Ministerio de Economía Y Competitividad (CTQ2014-55907-R to P.F., S.C.); FIRB Futuro in Ricerca from the Italian Ministero dell'Istruzione, dell'Universitá e della Ricerca (RBFR130VS5_001 to A.F.); Peruvian Programa Nacional de Innovación para la Competitividad y Productividad (382-PNICP-PIBA-2014 (to P.M. and A.F.)). Funding for open access charge: Institutional funding.ae974a485f413a2113503eed53cd6c53
10.1093/nar/gkv975
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