Fiche publication
Date publication
avril 2015
Journal
Nature
Auteurs
Membres identifiés du Cancéropôle Est :
Dr KLAHOLZ Bruno
Tous les auteurs :
Khatter H, Myasnikov AG, Natchiar SK, Klaholz BP
Lien Pubmed
Résumé
Ribosomes are translational machineries that catalyse protein synthesis. Ribosome structures from various species are known at the atomic level, but obtaining the structure of the human ribosome has remained a challenge; efforts to address this would be highly relevant with regard to human diseases. Here we report the near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building. The structure has an average resolution of 3.6 Å, reaching 2.9 Å resolution in the most stable regions. It provides unprecedented insights into ribosomal RNA entities and amino acid side chains, notably of the transfer RNA binding sites and specific molecular interactions with the exit site tRNA. It reveals atomic details of the subunit interface, which is seen to remodel strongly upon rotational movements of the ribosomal subunits. Furthermore, the structure paves the way for analysing antibiotic side effects and diseases associated with deregulated protein synthesis.
Mots clés
Binding Sites, Cryoelectron Microscopy, Electrons, Humans, Models, Molecular, RNA, Ribosomal, chemistry, RNA, Transfer, chemistry, Ribosomal Proteins, chemistry, Ribosome Subunits, chemistry, Ribosomes, chemistry
Référence
Nature. 2015 Apr 30;520(7549):640-5
