Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A.
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Ochoa Lizarralde, Borja
Connell, Sean R
Gualerzi, Claudio O
Protein Synthesis Inhibitors
RNA, Transfer, Amino Acyl
Ribosome Subunits, Large, Bacterial
MetadataShow full item record
CitationCrystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A. 2015, 43 (20):10015-25 Nucleic Acids Res.
PublisherOxford University Press
JournalNucleic acids research (Nucleic Acids Res.)
AbstractHygromycin 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.
SponsorsBizkaia: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.
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