1dm9
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(New page: 200px<br /><applet load="1dm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dm9, resolution 2.0Å" /> '''HEAT SHOCK PROTEIN 15...)
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Revision as of 11:17, 20 November 2007
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HEAT SHOCK PROTEIN 15 KD
Overview
We have solved the crystal structure of the heat shock protein Hsp15, a, newly isolated and very highly inducible heat shock protein that binds the, ribosome. Comparison of its structure with those of two RNA-binding, proteins, ribosomal protein S4 and threonyl-tRNA synthetase, reveals a, novel RNA-binding motif. This newly recognized motif is remarkably common, present in at least eight different protein families that bind RNA. The, motif's surface is populated by conserved, charged residues that define a, likely RNA-binding site. An intriguing pattern emerges: stress proteins, ribosomal proteins and tRNA synthetases repeatedly share a conserved, motif. This may imply a hitherto unrecognized functional similarity, between these three protein classes.
About this Structure
1DM9 is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Structure of Hsp15 reveals a novel RNA-binding motif., Staker BL, Korber P, Bardwell JC, Saper MA, EMBO J. 2000 Feb 15;19(4):749-57. PMID:10675344
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