Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome.
Fiche publication
Date publication
septembre 2016
Journal
Journal of molecular biology
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat, Dr YUSUPOVA Gulnara
Tous les auteurs :
Melnikov S, Mailliot J, Shin BS, Rigger L, Yusupova G, Micura R, Dever TE, Yusupov M
Lien Pubmed
Résumé
Eukaryotic translation initiation factor eIF5A promotes protein synthesis by resolving polyproline-induced ribosomal stalling. Here, we report a 3.25-Å resolution crystal structure of eIF5A bound to the yeast 80S ribosome. The structure reveals a previously unseen conformation of an eIF5A-ribosome complex and highlights a possible functional link between conformational changes of the ribosome during protein synthesis and the eIF5A-ribosome association.
Mots clés
Crystallography, X-Ray, Models, Molecular, Peptide Initiation Factors, chemistry, Protein Binding, Protein Biosynthesis, Protein Conformation, RNA-Binding Proteins, chemistry, Ribosomes, chemistry, Saccharomyces cerevisiae, chemistry
Référence
J. Mol. Biol.. 2016 09 11;428(18):3570-3576