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Title: Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex
Authors: Feng, Shu
Chen, Yun
Gao, Yong-Gui
Keywords: DRNTU::Science::Biological sciences::Microbiology
Issue Date: 2013
Source: Feng, S., Chen, Y., & Gao, Y. G. (2013). Crystal Structure of 70S Ribosome with Both Cognate tRNAs in the E and P Sites Representing an Authentic Elongation Complex. PLoS ONE, 8(3).
Series/Report no.: PLoS ONE
Abstract: During the translation cycle, a cognate deacylated tRNA can only move together with the codon into the E site. We here present the first structure of a cognate tRNA bound to the ribosomal E site resulting from translocation by EF-G, in which an entire L1 stalk (L1 protein and L1 rRNA) interacts with E-site tRNA (E-tRNA), representing an authentic ribosome elongation complex. Our results revealed that the Watson-Crick base pairing is formed at the first and second codon-anticodon positions in the E site in the ribosome elongation complex, whereas the codon-anticodon interaction in the third position is indirect. Analysis of the observed conformations of mRNA and E-tRNA suggests that the ribosome intrinsically has the potential to form codon-anticodon interaction in the E site, independently of the mRNA configuration. We also present a detailed description of the biologically relevant position of the entire L1 stalk and its interacting cognate E-tRNA, which provides a better understanding of the structural basis for translation elongation. Furthermore, to gain insight into translocation, we report the positioning of protein L6 contacting EF-G, as well as the conformational change of the Cterminal tail of protein S13 in the decoding center.
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0058829
Rights: © 2013 The Author(s).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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