2H50

Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26

2H50 の概要

• エントリーDOI: 10.2210/pdb2h50/pdb
• 関連するPDBエントリー: 1GME 2H53
• EMDBエントリー: 1221
• 分子名称: small heat shock protein Hsp26 (1 entity in total)
• 機能のキーワード: alpha-crystallin, chaperones, heat shock proteins, single particle reconstruction, chaperone
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 256324.13

構造登録者

White, H.E.,Orlova, E.V.,Chen, S.,Wang, L.,Ignatiou, A.,Gowen, B.,Stromer, T.,Franzmann, T.M.,Haslbeck, M.,Buchner, J.,Saibil, H.R. (登録日: 2006-05-25, 公開日: 2006-08-01, 最終更新日: 2024-02-14)

主引用文献

White, H.E.,Orlova, E.V.,Chen, S.,Wang, L.,Ignatiou, A.,Gowen, B.,Stromer, T.,Franzmann, T.M.,Haslbeck, M.,Buchner, J.,Saibil, H.R.
Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein hsp26
Structure, 14:1197-1204, 2006

PubMed Abstract: Small heat shock proteins are a superfamily of molecular chaperones that suppress protein aggregation and provide protection from cell stress. A key issue for understanding their action is to define the interactions of subunit domains in these oligomeric assemblies. Cryo-electron microscopy of yeast Hsp26 reveals two distinct forms, each comprising 24 subunits arranged in a porous shell with tetrahedral symmetry. The subunits form elongated, asymmetric dimers that assemble via trimeric contacts. Modifications of both termini cause rearrangements that yield a further four assemblies. Each subunit contains an N-terminal region, a globular middle domain, the alpha-crystallin domain, and a C-terminal tail. Twelve of the C termini form 3-fold assembly contacts which are inserted into the interior of the shell, while the other 12 C termini form contacts on the surface. Hinge points between the domains allow a variety of assembly contacts, providing the flexibility required for formation of supercomplexes with non-native proteins.

PubMed: 16843901
DOI: 10.1016/j.str.2006.05.021

実験手法

ELECTRON MICROSCOPY (10.8 Å)