EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.
ジャーナル・号・ページ	Structure, Vol. 14, Issue 7, Page 1197-1204, Year 2006
掲載日	2006年9月15日
著者	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 要旨	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.
リンク	Structure / PubMed:16843901
手法	EM (単粒子)
解像度	10.8 - 14.5 Å
構造データ	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 手法: EM (単粒子) / 解像度: 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 手法: EM (単粒子) / 解像度: 11.5 Å EMDB-1227: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. 手法: EM (単粒子) / 解像度: 14.2 Å EMDB-1228: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. 手法: EM (単粒子) / 解像度: 14.5 Å EMDB-1229: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. 手法: EM (単粒子) / 解像度: 12.6 Å EMDB-1230: Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. 手法: EM (単粒子) / 解像度: 14.2 Å
由来	saccharomyces cerevisiae (パン酵母)
キーワード	CHAPERONE / alpha-crystallin / chaperones / heat shock proteins / single particle reconstruction