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| | <StructureSection load='5ds1' size='340' side='right'caption='[[5ds1]], [[Resolution|resolution]] 2.63Å' scene=''> | | <StructureSection load='5ds1' size='340' side='right'caption='[[5ds1]], [[Resolution|resolution]] 2.63Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ds1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Garden_pea Garden pea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DS1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DS1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ds1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DS1 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP17.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3888 Garden pea])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.63Å</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=5ds1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ds1 OCA], [http://pdbe.org/5ds1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ds1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ds1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ds1 ProSAT]</span></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=5ds1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ds1 OCA], [https://pdbe.org/5ds1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ds1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ds1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ds1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HSP21_PEA HSP21_PEA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Garden pea]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allison, T A]] | + | [[Category: Pisum sativum]] |
| - | [[Category: Benesch, J L.P]] | + | [[Category: Allison TA]] |
| - | [[Category: Hochberg, G K.A]] | + | [[Category: Benesch JLP]] |
| - | [[Category: Laganoswky, A]] | + | [[Category: Hochberg GKA]] |
| - | [[Category: Shepherd, D A]] | + | [[Category: Laganoswky A]] |
| - | [[Category: Chaperone]] | + | [[Category: Shepherd DA]] |
| - | [[Category: Core domain]]
| + | |
| - | [[Category: Shsp]]
| + | |
| Structural highlights
Function
HSP21_PEA
Publication Abstract from PubMed
Oligomeric proteins assemble with exceptional selectivity, even in the presence of closely related proteins, to perform their cellular roles. We show that most proteins related by gene duplication of an oligomeric ancestor have evolved to avoid hetero-oligomerization and that this correlates with their acquisition of distinct functions. We report how coassembly is avoided by two oligomeric small heat-shock protein paralogs. A hierarchy of assembly, involving intermediates that are populated only fleetingly at equilibrium, ensures selective oligomerization. Conformational flexibility at noninterfacial regions in the monomers prevents coassembly, allowing interfaces to remain largely conserved. Homomeric oligomers must overcome the entropic benefit of coassembly and, accordingly, homomeric paralogs comprise fewer subunits than homomers that have no paralogs.
Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions.,Hochberg GKA, Shepherd DA, Marklund EG, Santhanagoplan I, Degiacomi MT, Laganowsky A, Allison TM, Basha E, Marty MT, Galpin MR, Struwe WB, Baldwin AJ, Vierling E, Benesch JLP Science. 2018 Feb 23;359(6378):930-935. doi: 10.1126/science.aam7229. PMID:29472485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hochberg GKA, Shepherd DA, Marklund EG, Santhanagoplan I, Degiacomi MT, Laganowsky A, Allison TM, Basha E, Marty MT, Galpin MR, Struwe WB, Baldwin AJ, Vierling E, Benesch JLP. Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions. Science. 2018 Feb 23;359(6378):930-935. doi: 10.1126/science.aam7229. PMID:29472485 doi:http://dx.doi.org/10.1126/science.aam7229
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