7VWX

CryoEM structure of football-shaped GroEL:ES2 with RuBisCO

7VWX の概要

• エントリーDOI: 10.2210/pdb7vwx/pdb
• EMDBエントリー: 32164
• 分子名称: Co-chaperonin GroES, Chaperonin GroEL, Ribulose bisphosphate carboxylase (3 entities in total)
• 機能のキーワード: chaperone, groel/es system, substrate folding, folding assistance
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 29
• 化学式量合計: 999636.00

構造登録者

Kim, H.,Roh, S.H. (登録日: 2021-11-12, 公開日: 2022-01-12, 最終更新日: 2024-11-13)

主引用文献

Kim, H.,Park, J.,Lim, S.,Jun, S.H.,Jung, M.,Roh, S.H.
Cryo-EM structures of GroEL:ES 2 with RuBisCO visualize molecular contacts of encapsulated substrates in a double-cage chaperonin.
Iscience, 25:103704-103704, 2022

PubMed Abstract: The GroEL/GroES chaperonin system assists the folding of many proteins, through conformational transitions driven by ATP hydrolysis. Although structural information about bullet-shaped GroEL:ES complexes has been extensively reported, the substrate interactions of another functional complex, the football-shaped GroEL:ES, remain elusive. Here, we report single-particle cryo-EM structures of reconstituted wild-type GroEL:ES complexes with a chemically denatured substrate, ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO). Our structures demonstrate that native-like folded RuBisCO density is captured at the lower part of the GroEL chamber and that GroEL's bulky hydrophobic residues Phe281, Tyr360, and Phe44 contribute to direct contact with RuBisCO density. In addition, our analysis found that GroEL:ES can be occupied by two substrates simultaneously, one in each chamber. Together, these observations provide insights to the football-shaped GroEL:ES complex as a functional state to assist the substrate folding with visualization.

PubMed: 35036883
DOI: 10.1016/j.isci.2021.103704

実験手法

ELECTRON MICROSCOPY (7.6 Å)