1gme
From Proteopedia
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| - | [[Image:1gme.jpg|left|200px]]<br /><applet load="1gme" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1gme, resolution 2.7Å" /> | ||
| - | '''CRYSTAL STRUCTURE AND ASSEMBLY OF AN EUKARYOTIC SMALL HEAT SHOCK PROTEIN'''<br /> | ||
| - | == | + | ==Crystal structure and assembly of an eukaryotic small heat shock protein== |
| + | <StructureSection load='1gme' size='340' side='right'caption='[[1gme]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1gme]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GME FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gme OCA], [https://pdbe.org/1gme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gme RCSB], [https://www.ebi.ac.uk/pdbsum/1gme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gme ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HS16B_WHEAT HS16B_WHEAT] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/1gme_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gme ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The 2.7 A structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its alpha-crystallin domain and flanking extensions assemble into a dodecameric double disk. The folding of the monomer and assembly of the oligomer are mutually interdependent, involving strand exchange, helix swapping, loose knots and hinged extensions. In support of the chaperone mechanism, the substrate-bound dimers, in temperature-dependent equilibrium with higher assembly forms, have unfolded N-terminal arms and exposed conserved hydrophobic binding sites on the alpha-crystallin domain. The structure also provides a model by which members of the sHSP protein family bind unfolded substrates, which are involved in a variety of neurodegenerative diseases and cataract formation. | The 2.7 A structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its alpha-crystallin domain and flanking extensions assemble into a dodecameric double disk. The folding of the monomer and assembly of the oligomer are mutually interdependent, involving strand exchange, helix swapping, loose knots and hinged extensions. In support of the chaperone mechanism, the substrate-bound dimers, in temperature-dependent equilibrium with higher assembly forms, have unfolded N-terminal arms and exposed conserved hydrophobic binding sites on the alpha-crystallin domain. The structure also provides a model by which members of the sHSP protein family bind unfolded substrates, which are involved in a variety of neurodegenerative diseases and cataract formation. | ||
| - | + | Crystal structure and assembly of a eukaryotic small heat shock protein.,van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E Nat Struct Biol. 2001 Dec;8(12):1025-30. PMID:11702068<ref>PMID:11702068</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1gme" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Triticum aestivum]] | ||
| + | [[Category: Basha E]] | ||
| + | [[Category: Friedrich KL]] | ||
| + | [[Category: Slingsby C]] | ||
| + | [[Category: Van Montfort RLM]] | ||
| + | [[Category: Vierling E]] | ||
Current revision
Crystal structure and assembly of an eukaryotic small heat shock protein
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