Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.
Journal, issue, pages	Structure, Vol. 14, Issue 7, Page 1197-1204, Year 2006
Publish date	Sep 15, 2006
Authors	Helen E White / Elena V Orlova / Shaoxia Chen / Luchun Wang / Athanasios Ignatiou / Brent Gowen / Thusnelda Stromer / Titus M Franzmann / Martin Haslbeck / Johannes Buchner / Helen R Saibil /
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 ...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.
External links	Structure / PubMed:16843901
Methods	EM (single particle)
Resolution	10.8 - 14.5 Å
Structure data	1221 2h50 EMDB-1221: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. PDB-2h50: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26 Method: EM (single particle) / Resolution: 10.8 Å 1226 2h53 EMDB-1226: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. PDB-2h53: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26 Method: EM (single particle) / Resolution: 11.5 Å EMDB-1227: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Method: EM (single particle) / Resolution: 14.2 Å EMDB-1228: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Method: EM (single particle) / Resolution: 14.5 Å EMDB-1229: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Method: EM (single particle) / Resolution: 12.6 Å EMDB-1230: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Method: EM (single particle) / Resolution: 14.2 Å
Source	saccharomyces cerevisiae (brewer's yeast)
Keywords	CHAPERONE / alpha-crystallin / chaperones / heat shock proteins / single particle reconstruction