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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
|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.||URI:||https://hdl.handle.net/10356/96532
|ISSN:||1932-6203||DOI:||http://dx.doi.org/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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