5DS2

Core domain of the class I small heat-shock protein HSP 18.1 from Pisum sativum

5DS2 の概要

• エントリーDOI: 10.2210/pdb5ds2/pdb
• 分子名称: 18.1 kDa class I heat shock protein, SULFATE ION (3 entities in total)
• 機能のキーワード: chaperone, small heat-shock protein, stress
• 由来する生物種: Pisum sativum (Garden pea)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 67629.88

構造登録者

Shepherd, D.A.,Laganowsky, A.,Allison, T.M.,Hochberg, G.K.A.,Benesch, J.L.P. (登録日: 2015-09-16, 公開日: 2016-09-28, 最終更新日: 2024-01-10)

主引用文献

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

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: 29472485
DOI: 10.1126/science.aam7229

実験手法

X-RAY DIFFRACTION (1.85 Å)