5DS1
Core domain of the class II small heat-shock protein HSP 17.7 from Pisum sativum
Summary for 5DS1
| Entry DOI | 10.2210/pdb5ds1/pdb |
| Descriptor | 17.1 kDa class II heat shock protein (2 entities in total) |
| Functional Keywords | shsp, chaperone, core domain |
| Biological source | Pisum sativum (Garden pea) |
| Total number of polymer chains | 3 |
| Total formula weight | 31941.73 |
| Authors | Hochberg, G.K.A.,Laganoswky, A.,Allison, T.A.,Shepherd, D.A.,Benesch, J.L.P. (deposition date: 2015-09-16, release date: 2016-09-28, Last modification date: 2024-01-10) |
| Primary citation | Hochberg, G.K.A.,Shepherd, D.A.,Marklund, E.G.,Santhanagoplan, I.,Degiacomi, M.T.,Laganowsky, A.,Allison, T.M.,Basha, E.,Marty, M.T.,Galpin, M.R.,Struwe, W.B.,Baldwin, A.J.,Vierling, E.,Benesch, J.L.P. Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions. Science, 359:930-935, 2018 Cited by PubMed Abstract: 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. PubMed: 29472485DOI: 10.1126/science.aam7229 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.63 Å) |
Structure validation
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