1pkp
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(New page: 200px<br /><applet load="1pkp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pkp, resolution 2.8Å" /> '''THE STRUCTURE OF RIBO...)
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Revision as of 21:46, 20 November 2007
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THE STRUCTURE OF RIBOSOMAL PROTEIN S5 REVEALS SITES OF INTERACTION WITH 16S RRNA
Overview
Understanding the process whereby the ribosome translates the genetic code, into protein molecules will ultimately require high-resolution structural, information, and we report here the first crystal structure of a protein, from the small ribosomal subunit. This protein, S5, has a molecular mass, of 17,500 and is highly conserved in all lifeforms. The molecule contains, two distinct alpha/beta domains that have structural similarities to, several other proteins that are components of ribonucleoprotein complexes., Mutations in S5 result in several phenotypes which suggest that S5 may, have a role in translational fidelity and translocation. These include, ribosome ambiguity or ram, reversion from streptomycin dependence and, resistance to spectinomycin. Also, a cold-sensitive, spectinomycin-resistant mutant of S5 has been identified which is, defective in initiation. Here we show that these mutations map to two, distinct regions of the molecule which seem to be sites of interaction, with ribosomal RNA. A structure/function analysis of the molecule reveals, discrepancies with current models of the 30S subunit.
About this Structure
1PKP is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA., Ramakrishnan V, White SW, Nature. 1992 Aug 27;358(6389):768-71. PMID:1508272
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