The structure of the ribosome with elongation factor G trapped in the posttranslocational state
2009 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 326, no 5953, 694-699 p.Article in journal (Refereed) Published
Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during translation by the ribosome. We report a crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid. Fusidic acid traps EF-G in a conformation intermediate between the guanosine triphosphate and guanosine diphosphate forms. The interaction of EF-G with ribosomal elements implicated in stimulating catalysis, such as the L10-L12 stalk and the L11 region, and of domain IV of EF-G with the tRNA at the peptidyl-tRNA binding site (P site) and with mRNA shed light on the role of these elements in EF-G function. The stabilization of the mobile stalks of the ribosome also results in a more complete description of its structure.
Place, publisher, year, edition, pages
2009. Vol. 326, no 5953, 694-699 p.
IdentifiersURN: urn:nbn:se:uu:diva-141781DOI: 10.1126/science.1179709PubMedID: 19833919OAI: oai:DiVA.org:uu-141781DiVA: diva2:386223