4V8U

Crystal Structure of 70S Ribosome with Both Cognate tRNAs in the E and P Sites Representing an Authentic Elongation Complex.

This is a non-PDB format compatible entry.

Summary for 4V8U

• Entry DOI: 10.2210/pdb4v8u/pdb
• Descriptor: 16S RIBOSOMAL RNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (61 entities in total)
• Functional Keywords: ribosome, protein translation
• Biological source: THERMUS THERMOPHILUS HB8; More
• Total number of polymer chains: 114
• Total formula weight: 4655336.07

Authors

Gao, Y.G.,Feng, S.,Chen, Y. (deposition date: 2012-08-28, release date: 2014-07-09, Last modification date: 2024-10-09)

Primary citation

Feng, S.,Chen, Y.,Gao, Y.G.
Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex.
PLoS ONE, 8:e58829-e58829, 2013

PubMed 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 C-terminal tail of protein S13 in the decoding center.

PubMed: 23527033
DOI: 10.1371/journal.pone.0058829

Experimental method

X-RAY DIFFRACTION (3.7 Å)