4ylb: Difference between revisions
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''' | ==Crystal Structure of A102D mutant of hsp14.1 from Sulfolobus solfatataricus P2== | ||
<StructureSection load='4ylb' size='340' side='right' caption='[[4ylb]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ylb]] is a 4 chain structure. 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> | |||
</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> | |||
<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'>[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]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:26439766</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ylb" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chen, J Y]] | |||
[[Category: Liu, L]] | [[Category: Liu, L]] | ||
[[Category: Yun, C | [[Category: Yun, C H]] | ||
[[Category: | [[Category: Chaperone]] | ||
[[Category: Molecular chaperone]] | |||
[[Category: Small heat shock protein]] | |||
[[Category: Sshsp14 1]] | |||
Revision as of 22:31, 30 November 2015
Crystal Structure of A102D mutant of hsp14.1 from Sulfolobus solfatataricus P2Crystal Structure of A102D mutant 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. References
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