1dm9
From Proteopedia
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|PDB= 1dm9 |SIZE=350|CAPTION= <scene name='initialview01'>1dm9</scene>, resolution 2.0Å | |PDB= 1dm9 |SIZE=350|CAPTION= <scene name='initialview01'>1dm9</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm9 OCA], [http://www.ebi.ac.uk/pdbsum/1dm9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dm9 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Saper, M A.]] | [[Category: Saper, M A.]] | ||
[[Category: Staker, B L.]] | [[Category: Staker, B L.]] | ||
| - | [[Category: SO4]] | ||
[[Category: heat shock protein]] | [[Category: heat shock protein]] | ||
[[Category: protein-rna interaction]] | [[Category: protein-rna interaction]] | ||
[[Category: ribosome]] | [[Category: ribosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:44:22 2008'' |
Revision as of 16:44, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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