2bol: Difference between revisions
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<StructureSection load='2bol' size='340' side='right' caption='[[2bol]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2bol' size='340' side='right' caption='[[2bol]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bol]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2bol]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Beef_tapeworm Beef tapeworm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BOL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2bol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bol RCSB], [http://www.ebi.ac.uk/pdbsum/2bol PDBsum]</span></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=2bol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bol OCA], [http://pdbe.org/2bol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bol RCSB], [http://www.ebi.ac.uk/pdbsum/2bol PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/TSP36_TAESA TSP36_TAESA]] Has chaperone activity towards unfolded proteins (in vitro).<ref>PMID:15326597</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2bol" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Beef tapeworm]] | ||
[[Category: Boelens, W C]] | [[Category: Boelens, W C]] | ||
[[Category: Kappe, G]] | [[Category: Kappe, G]] | ||
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[[Category: Molecular chaperone]] | [[Category: Molecular chaperone]] | ||
[[Category: Small heat shock protein]] | [[Category: Small heat shock protein]] | ||
[[Category: Taenia saginata]] | |||
Revision as of 03:31, 10 September 2015
CRYSTAL STRUCTURE AND ASSEMBLY OF TSP36, A METAZOAN SMALL HEAT SHOCK PROTEINCRYSTAL STRUCTURE AND ASSEMBLY OF TSP36, A METAZOAN SMALL HEAT SHOCK PROTEIN
Structural highlights
Function[TSP36_TAESA] Has chaperone activity towards unfolded proteins (in vitro).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSmall heat shock proteins (sHsps) are oligomers that perform a protective function by binding denatured proteins. Although ubiquitous, they are of variable sequence except for a C-terminal approximately 90-residue "alpha-crystallin domain". Unlike larger stress response chaperones, sHsps are ATP-independent and generally form polydisperse assemblies. One proposed mechanism of action involves these assemblies breaking into smaller subunits in response to stress, before binding unfolding substrate and reforming into larger complexes. Two previously solved non-metazoan sHsp multimers are built from dimers formed by domain swapping between the alpha-crystallin domains, adding to evidence that the smaller subunits are dimers. Here, the 2.5A resolution structure of an sHsp from the parasitic flatworm Taenia saginata Tsp36, the first metazoan crystal structure, shows a new mode of dimerization involving N-terminal regions, which differs from that seen for non-metazoan sHsps. Sequence differences in the alpha-crystallin domains between metazoans and non-metazoans are critical to the different mechanism of dimerization, suggesting that some structural features seen for Tsp36 may be generalized to other metazoan sHsps. The structure also indicates scope for flexible assembly of subunits, supporting the proposed process of oligomer breakdown, substrate binding and reassembly as the chaperone mechanism. It further shows how sHsps can bind coil and secondary structural elements by wrapping them around the alpha-crystallin domain. The structure also illustrates possible roles for conserved residues associated with disease, and suggests a mechanism for the sHsp-related pathogenicity of some flatworm infections. Tsp36, like other flatworm sHsps, possesses two divergent sHsp repeats per monomer. Together with the two previously solved structures, a total of four alpha-crystallin domain structures are now available, giving a better definition of domain boundaries for sHsps. Wrapping the alpha-crystallin domain fold in a chaperone assembly.,Stamler R, Kappe G, Boelens W, Slingsby C J Mol Biol. 2005 Oct 14;353(1):68-79. PMID:16165157[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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