8WU4

Cryo-EM structure of native H. thermoluteolus TH-1 GroEL

8WU4 の概要

• エントリーDOI: 10.2210/pdb8wu4/pdb
• EMDBエントリー: 37850
• 分子名称: Chaperonin GroEL (1 entity in total)
• 機能のキーワード: chaperone, chaperonin, atpase, protein folding
• 由来する生物種: Hydrogenophilus thermoluteolus
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 781718.98

構造登録者

Liao, Z.,Gopalasingam, C.C.,Kameya, M.,Gerle, C.,Shigematsu, H.,Ishii, M.,Arakawa, T.,Fushinobu, S. (登録日: 2023-10-20, 公開日: 2024-03-27, 最終更新日: 2024-06-19)

主引用文献

Liao, Z.,Gopalasingam, C.C.,Kameya, M.,Gerle, C.,Shigematsu, H.,Ishii, M.,Arakawa, T.,Fushinobu, S.
Structural insights into thermophilic chaperonin complexes.
Structure, 32:679-689.e4, 2024

PubMed Abstract: Group I chaperonins are dual heptamer protein complexes that play significant roles in protein homeostasis. The structure and function of the Escherichia coli chaperonin are well characterized. However, the dynamic properties of chaperonins, such as large ATPase-dependent conformational changes by binding of lid-like co-chaperonin GroES, have made structural analyses challenging, and our understanding of these changes during the turnover of chaperonin complex formation is limited. In this study, we used single-particle cryogenic electron microscopy to investigate the structures of GroES-bound chaperonin complexes from the thermophilic hydrogen-oxidizing bacteria Hydrogenophilus thermoluteolus and Hydrogenobacter thermophilus in the presence of ATP and AMP-PNP. We captured the structure of an intermediate state chaperonin complex, designated as an asymmetric football-shaped complex, and performed analyses to decipher the dynamic structural variations. Our structural analyses of inter- and intra-subunit communications revealed a unique mechanism of complex formation through the binding of a second GroES to a bullet-shaped complex.

PubMed: 38492570
DOI: 10.1016/j.str.2024.02.012

実験手法

ELECTRON MICROSCOPY (3.3 Å)