2h50

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Revision as of 18:14, 29 January 2008

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

Overview

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.

About this Structure

2H50 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26., White HE, Orlova EV, Chen S, Wang L, Ignatiou A, Gowen B, Stromer T, Franzmann TM, Haslbeck M, Buchner J, Saibil HR, Structure. 2006 Jul;14(7):1197-204. PMID:16843901

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