Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A.
Average rating
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Star rating
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Authors
Kaminishi, TatsuyaSchedlbauer, Andreas
Fabbretti, Attilio
Brandi, Letizia
Ochoa Lizarralde, Borja
He, Cheng-Guang
Milon, Pohl
Connell, Sean R
Gualerzi, Claudio O
Fucini, Paola
Issue Date
2015-11-16Keywords
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]
Metadata
Show full item recordCitation
Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A. 2015, 43 (20):10015-25 Nucleic Acids Res.Publisher
Oxford University PressJournal
Nucleic acids research (Nucleic Acids Res.)DOI
10.1093/nar/gkv975PubMed ID
26464437Additional Links
http://nar.oxfordjournals.org/content/43/20/10015.longAbstract
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.Type
info:eu-repo/semantics/articleRights
info:eu-repo/semantics/openAccessLanguage
engISSN
1362-4962Sponsors
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
Scopus Count
Collections
The following license files are associated with this item:
- Creative Commons
Related articles
- Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A.
- Authors: Polikanov YS, Starosta AL, Juette MF, Altman RB, Terry DS, Lu W, Burnett BJ, Dinos G, Reynolds KA, Blanchard SC, Steitz TA, Wilson DN
- Issue date: 2015 Jun 4
- Inhibition of the ribosomal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin.
- Authors: Poulsen SM, Kofoed C, Vester B
- Issue date: 2000 Dec 1
- Role of ribosomal protein L27 in peptidyl transfer.
- Authors: Trobro S, Aqvist J
- Issue date: 2008 Apr 29
- The site of action of oxazolidinone antibiotics in living bacteria and in human mitochondria.
- Authors: Leach KL, Swaney SM, Colca JR, McDonald WG, Blinn JR, Thomasco LM, Gadwood RC, Shinabarger D, Xiong L, Mankin AS
- Issue date: 2007 May 11
- The inhibitory mechanism of protein synthesis by YoeB, an Escherichia coli toxin.
- Authors: Zhang Y, Inouye M
- Issue date: 2009 Mar 13