3ZQ0

Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein

3ZQ0 の概要

• エントリーDOI: 10.2210/pdb3zq0/pdb
• 関連するPDBエントリー: 3ZPZ 3ZQ1
• EMDBエントリー: 2326
• 分子名称: 60 KDA CHAPERONIN, 10 KDA CHAPERONIN, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: protein folding, heterogeneity, encapsulation
• 由来する生物種: ESCHERICHIA COLI BL21; 詳細
• 細胞内の位置: Cytoplasm : P0A6F5 P0A6F9
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 849048.58

構造登録者

Chen, D.-H.,Madan, D.,Weaver, J.,Lin, Z.,Schroder, G.F.,Chiu, W.,Rye, H.S. (登録日: 2013-03-04, 公開日: 2013-06-19, 最終更新日: 2024-05-08)

主引用文献

Chen, D.-H.,Madan, D.,Weaver, J.,Lin, Z.,Schroder, G.F.,Chiu, W.,Rye, H.S.
Visualizing Groel/Es in the Act of Encapsulating a Folding Protein
Cell(Cambridge,Mass.), 153:1354-, 2013

PubMed Abstract: 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.

PubMed: 23746846
DOI: 10.1016/J.CELL.2013.04.052

実験手法

ELECTRON MICROSCOPY (9.2 Å)