1dm9
From Proteopedia
(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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| - | [[Image:1dm9.gif|left|200px]]<br /><applet load="1dm9" size=" | + | [[Image:1dm9.gif|left|200px]]<br /><applet load="1dm9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dm9, resolution 2.0Å" /> | caption="1dm9, resolution 2.0Å" /> | ||
'''HEAT SHOCK PROTEIN 15 KD'''<br /> | '''HEAT SHOCK PROTEIN 15 KD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have solved the crystal structure of the heat shock protein Hsp15, a | + | 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== | ==About this Structure== | ||
| - | 1DM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DM9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bardwell, J | + | [[Category: Bardwell, J C.A.]] |
[[Category: Korber, P.]] | [[Category: Korber, P.]] | ||
| - | [[Category: Saper, M | + | [[Category: Saper, M A.]] |
| - | [[Category: Staker, B | + | [[Category: Staker, B L.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: heat shock proteins]] | [[Category: heat shock proteins]] | ||
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[[Category: ribosome]] | [[Category: ribosome]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:09 2008'' |
Revision as of 10:18, 21 February 2008
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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 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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