The structure of the ribosome with elongation factor G trapped in the posttranslocational state.
Yong-Gui Gao,Maria Selmer,Christine M. Dunham,Albert Weixlbaumer,Ann C. Kelley,Venki Ramakrishnan +5 more
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TLDR
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 is reported, providing insights into translocation and decoding.Abstract:
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.read more
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What recent ribosome structures have revealed about the mechanism of translation
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Andreas M. Anger,Jean Paul Armache,Otto Berninghausen,Michael Habeck,Marion Subklewe,Daniel N. Wilson,Roland Beckmann +6 more
TL;DR: In this paper, the structure of metazoan 80S ribosomes with the translation factor eEF2, E-site transfer RNA and Stm1-like proteins has been determined.
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The Elongation, Termination, and Recycling Phases of Translation in Eukaryotes
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References
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疟原虫var基因转换速率变化导致抗原变异[英]/Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A
TL;DR: PfPMP1)与感染红细胞、树突状组胞以及胎盘的单个或多个受体作用,在黏附及免疫逃避中起关键的作�ly.
Journal ArticleDOI
Structures of the bacterial ribosome at 3.5 Å resolution
Barbara S Schuwirth,Maria A. Borovinskaya,Cathy W Hau,Wen Zhang,Antón Vila-Sanjurjo,James M. Holton,Jamie H. D. Cate,Jamie H. D. Cate +7 more
TL;DR: Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA and transfer RNAs during translocation.
Journal ArticleDOI
Structure of the 70S Ribosome Complexed with mRNA and tRNA
Maria Selmer,Christine M. Dunham,Frank V. Murphy,Albert Weixlbaumer,Sabine Petry,Ann C. Kelley,John R. Weir,Venki Ramakrishnan +7 more
TL;DR: The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (t RNA) and metal ions also stabilize the intersubunit interface.
Journal ArticleDOI
Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit
James M. Ogle,Ditlev E. Brodersen,William M. Clemons,Michael J. Tarry,Andrew P. Carter,Venki Ramakrishnan +5 more
TL;DR: Crystal structures of the 30S ribosomal subunit in complex with messenger RNA and cognate transfer RNA in the A site, both in the presence and absence of the antibiotic paromomycin, have been solved at between 3.1 and 3.3 angstroms resolution.