+検索条件
-Structure paper
タイトル | Visualizing GroEL/ES in the act of encapsulating a folding protein. |
---|---|
ジャーナル・号・ページ | Cell, Vol. 153, Issue 6, Page 1354-1365, Year 2013 |
掲載日 | 2013年6月6日 |
著者 | Dong-Hua Chen / Damian Madan / Jeremy Weaver / Zong Lin / Gunnar F Schröder / Wah Chiu / Hays S Rye / |
PubMed 要旨 | The GroEL/ES chaperonin system is required for the assisted folding of many proteins. How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood. Using symmetry- ...The GroEL/ES chaperonin system is required for the assisted folding of many proteins. How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood. Using symmetry-free, single-particle cryo-electron microscopy, we have characterized a chemically modified mutant of GroEL (EL43Py) that is trapped at a normally transient stage of substrate protein encapsulation. We show that the symmetric pattern of the GroEL subunits is broken as the GroEL cis-ring apical domains reorient to accommodate the simultaneous binding of GroES and an incompletely folded substrate protein (RuBisCO). The collapsed RuBisCO folding intermediate binds to the lower segment of two apical domains, as well as to the normally unstructured GroEL C-terminal tails. A comparative structural analysis suggests that the allosteric transitions leading to substrate protein release and folding involve concerted shifts of GroES and the GroEL apical domains and C-terminal tails. |
リンク | Cell / PubMed:23746846 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 8.9 - 15.9 Å |
構造データ | EMDB-2325: Visualizing GroEL/ES in the Act of Encapsulating a Non-Native Substrate Protein |
化合物 | ChemComp-MG: ChemComp-ADP: |
由来 |
|
キーワード | CHAPERONE (シャペロン) / PROTEIN FOLDING (フォールディング) / HETEROGENEITY / ENCAPSULATION / RUBISCO (リブロース1,5-ビスリン酸カルボキシラーゼ/オキシゲナーゼ) |