1ibm

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Revision as of 15:08, 20 November 2007

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spinqualitylabelsall models 1ibm, resolution 3.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH A MESSENGER RNA FRAGMENT AND COGNATE TRANSFER RNA ANTICODON STEM-LOOP BOUND AT THE A SITE

Overview

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. Cognate transfer RNA (tRNA) binding induces, global domain movements of the 30S subunit and changes in the conformation, of the universally conserved and essential bases A1492, A1493, and G530 of, 16S RNA. These bases interact intimately with the minor groove of the, first two base pairs between the codon and anticodon, thus sensing, Watson-Crick base-pairing geometry and discriminating against near-cognate, tRNA. The third, or "wobble," position of the codon is free to accommodate, certain noncanonical base pairs. By partially inducing these structural, changes, paromomycin facilitates binding of near-cognate tRNAs.

About this Structure

1IBM is a Protein complex structure of sequences from Thermus thermophilus with MG and ZN as ligands. Full crystallographic information is available from OCA.

Reference

Recognition of cognate transfer RNA by the 30S ribosomal subunit., Ogle JM, Brodersen DE, Clemons WM Jr, Tarry MJ, Carter AP, Ramakrishnan V, Science. 2001 May 4;292(5518):897-902. PMID:11340196

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