4yl9: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of wild-type of hsp14.1 from Sulfolobus solfatataricus P2== | ==Crystal Structure of wild-type of hsp14.1 from Sulfolobus solfatataricus P2== | ||
<StructureSection load='4yl9' size='340' side='right' caption='[[4yl9]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='4yl9' size='340' side='right'caption='[[4yl9]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yl9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YL9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YL9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4yl9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacs9 Sacs9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YL9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YL9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ylb|4ylb]], [[4ylc|4ylc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ylb|4ylb]], [[4ylc|4ylc]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yl9 OCA], [http://pdbe.org/4yl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yl9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yl9 PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ssol_0413 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=555311 SACS9])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yl9 OCA], [http://pdbe.org/4yl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yl9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yl9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yl9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 16: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4yl9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4yl9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Heat Shock Proteins|Heat Shock Proteins]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Sacs9]] | |||
[[Category: Chen, J Y]] | [[Category: Chen, J Y]] | ||
[[Category: Liu, L]] | [[Category: Liu, L]] | ||
Revision as of 10:16, 12 June 2019
Crystal Structure of wild-type of hsp14.1 from Sulfolobus solfatataricus P2Crystal Structure of wild-type of hsp14.1 from Sulfolobus solfatataricus P2
Structural highlights
Publication Abstract from PubMedSmall heat-shock proteins (sHsps) maintain cellular homeostasis by binding to denatured client proteins to prevent aggregation. Numerous studies indicate that the N-terminal domain (NTD) of sHsps is responsible for binding to client proteins, but the binding mechanism and chaperone activity regulation remain elusive. Here, we report the crystal structures of the wild-type and mutants of an sHsp from Sulfolobus solfataricus representing the inactive and active state of this protein, respectively. All three structures reveal well-defined NTD, but their conformations are remarkably different. The mutant NTDs show disrupted helices presenting a reformed hydrophobic surface compatible with recognizing client proteins. Our functional data show that mutating key hydrophobic residues in this region drastically altered the chaperone activity of this sHsp. These data suggest a new model in which a molecular switch located in NTD facilitates conformational changes for client protein binding. Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function.,Liu L, Chen JY, Yang B, Wang FH, Wang YH, Yun CH Structure. 2015 Nov 3;23(11):2066-75. doi: 10.1016/j.str.2015.08.015. Epub 2015, Oct 1. PMID:26439766[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||