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4ylc

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<StructureSection load='4ylc' size='340' side='right'caption='[[4ylc]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='4ylc' size='340' side='right'caption='[[4ylc]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ylc]] is a 8 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=4YLC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YLC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ylc]] is a 8 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=4YLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YLC FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yl9|4yl9]], [[4ylb|4ylb]]</td></tr>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ylc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ylc OCA], [https://pdbe.org/4ylc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ylc RCSB], [https://www.ebi.ac.uk/pdbsum/4ylc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ylc ProSAT]</span></td></tr>
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<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=4ylc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ylc OCA], [http://pdbe.org/4ylc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ylc RCSB], [http://www.ebi.ac.uk/pdbsum/4ylc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ylc ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D0KNS6_SACS9 D0KNS6_SACS9]
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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.
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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<ref>PMID:26439766</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ylc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Heat Shock Proteins|Heat Shock Proteins]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sacs9]]
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[[Category: Saccharolobus solfataricus 98/2]]
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[[Category: Chen, J Y]]
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[[Category: Chen JY]]
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[[Category: Liu, L]]
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[[Category: Liu L]]
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[[Category: Yun, C H]]
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[[Category: Yun CH]]
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[[Category: Chaperone]]
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[[Category: Molecular chaperone]]
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[[Category: Small heat shock protein]]
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[[Category: Sshsp14 1]]
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Current revision

Crystal Structure of Del-C4 mutant of hsp14.1 from Sulfolobus solfatataricus P2

PDB ID 4ylc

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