1y39

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1y39, resolution 2.80Å

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Co-evolution of protein and RNA structures within a highly conserved ribosomal domain

Overview

The X-ray crystal structure of a ribosomal L11-rRNA complex with, chloroplast-like mutations in both protein and rRNA is presented. The, global structure is almost identical to that of the wild-type (bacterial), complex, with only a small movement of the protein alpha helix away from, the surface of the RNA required to accommodate the altered protein, residue. In contrast, the specific hydrogen bonding pattern of the mutated, residues is substantially different, and now includes a direct interaction, between the protein side chain and an RNA base edge and a water-mediated, contact. Comparison of the two structures allows the observations of, sequence variation and relative affinities of wild-type and mutant, complexes to be clearly rationalized, but reinforces the concept that, there is no single simple code for protein-RNA recognition.

About this Structure

1Y39 is a Single protein structure of sequence from Geobacillus stearothermophilus with 3CO, K, MG and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Coevolution of protein and RNA structures within a highly conserved ribosomal domain., Dunstan MS, Guhathakurta D, Draper DE, Conn GL, Chem Biol. 2005 Feb;12(2):201-6. PMID:15734647

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