The structure of the ribosome with elongation factor G trapped in the posttranslocational state.
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.
Gao
Yong-Gui
YG
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK.
Selmer
Maria
M
Dunham
Christine M
CM
Weixlbaumer
Albert
A
Kelley
Ann C
AC
Ramakrishnan
V
V
D001426:Bacterial Proteins / Q000737:chemistry; D002384:Catalysis; D018360:Crystallography, X-Ray; D005672:Fusidic Acid / Q000737:chemistry / Q000494:pharmacology; D008958:Models, Molecular; D020653:Peptide Elongation Factor G / Q000737:chemistry*; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011500:Protein Synthesis Inhibitors / Q000737:chemistry / Q000494:pharmacology; D012329:RNA, Bacterial / Q000737:chemistry; D012333:RNA, Messenger / Q000737:chemistry; D012343:RNA, Transfer / Q000737:chemistry; D012270:Ribosomes / Q000737:chemistry*; D016963:Thermus thermophilus
D001426:Bacterial Proteins; D020653:Peptide Elongation Factor G; D011500:Protein Synthesis Inhibitors; D012329:RNA, Bacterial; D012333:RNA, Messenger; D005672:Fusidic Acid; D012343:RNA, Transfer