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4V87

Crystal structure analysis of ribosomal decoding.

This is a non-PDB format compatible entry.
Summary for 4V87
Entry DOI10.2210/pdb4v87/pdb
DescriptorRNA (2909-MER), 50S ribosomal protein L14, 50S ribosomal protein L15, ... (56 entities in total)
Functional Keywordsrna, ribosome, trna, translation, mrna
Biological sourceThermus thermophilus
More
Total number of polymer chains110
Total formula weight4496541.31
Authors
Demeshkina, N.,Jenner, L.,Yusupov, M.,Yusupova, G. (deposition date: 2011-09-20, release date: 2014-07-09, Last modification date: 2024-11-20)
Primary citationDemeshkina, N.,Jenner, L.,Westhof, E.,Yusupov, M.,Yusupova, G.
A new understanding of the decoding principle on the ribosome.
Nature, 484:256-259, 2012
Cited by
PubMed Abstract: During protein synthesis, the ribosome accurately selects transfer RNAs (tRNAs) in accordance with the messenger RNA (mRNA) triplet in the decoding centre. tRNA selection is initiated by elongation factor Tu, which delivers tRNA to the aminoacyl tRNA-binding site (A site) and hydrolyses GTP upon establishing codon-anticodon interactions in the decoding centre. At the following proofreading step the ribosome re-examines the tRNA and rejects it if it does not match the A codon. It was suggested that universally conserved G530, A1492 and A1493 of 16S ribosomal RNA, critical for tRNA binding in the A site, actively monitor cognate tRNA, and that recognition of the correct codon-anticodon duplex induces an overall ribosome conformational change (domain closure). Here we propose an integrated mechanism for decoding based on six X-ray structures of the 70S ribosome determined at 3.1-3.4 Å resolution, modelling cognate or near-cognate states of the decoding centre at the proofreading step. We show that the 30S subunit undergoes an identical domain closure upon binding of either cognate or near-cognate tRNA. This conformational change of the 30S subunit forms a decoding centre that constrains the mRNA in such a way that the first two nucleotides of the A codon are limited to form Watson-Crick base pairs. When U·G and G·U mismatches, generally considered to form wobble base pairs, are at the first or second codon-anticodon position, the decoding centre forces this pair to adopt the geometry close to that of a canonical C·G pair. This by itself, or with distortions in the codon-anticodon mini-helix and the anticodon loop, causes the near-cognate tRNA to dissociate from the ribosome.
PubMed: 22437501
DOI: 10.1038/nature10913
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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