|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4ylb' size='340' side='right'caption='[[4ylb]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='4ylb' size='340' side='right'caption='[[4ylb]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ylb]] 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=4YLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YLB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ylb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_98/2 Saccharolobus solfataricus 98/2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YLB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yl9|4yl9]], [[4ylc|4ylc]]</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=4ylb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ylb OCA], [https://pdbe.org/4ylb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ylb RCSB], [https://www.ebi.ac.uk/pdbsum/4ylb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ylb ProSAT]</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=4ylb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ylb OCA], [http://pdbe.org/4ylb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ylb RCSB], [http://www.ebi.ac.uk/pdbsum/4ylb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ylb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D0KNS6_SACS9 D0KNS6_SACS9] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 20: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Heat Shock Proteins|Heat Shock Proteins]] | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 26: |
Line 26: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sacs9]] | + | [[Category: Saccharolobus solfataricus 98/2]] |
| - | [[Category: Chen, J Y]] | + | [[Category: Chen JY]] |
| - | [[Category: Liu, L]] | + | [[Category: Liu L]] |
| - | [[Category: Yun, C H]] | + | [[Category: Yun CH]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Molecular chaperone]]
| + | |
| - | [[Category: Small heat shock protein]]
| + | |
| - | [[Category: Sshsp14 1]]
| + | |
| Structural highlights
Function
D0KNS6_SACS9
Publication Abstract from PubMed
Small 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 Also
References
- ↑ Liu L, Chen JY, Yang B, Wang FH, Wang YH, Yun CH. Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function. Structure. 2015 Nov 3;23(11):2066-75. doi: 10.1016/j.str.2015.08.015. Epub 2015, Oct 1. PMID:26439766 doi:http://dx.doi.org/10.1016/j.str.2015.08.015
|
