3J1C

Cryo-EM structure of 9-fold symmetric rATcpn-alpha in apo state

3J1C の概要

• エントリーDOI: 10.2210/pdb3j1c/pdb
• 関連するPDBエントリー: 3J1B 3J1D 3J1E 3J1F 3J1G 3J1H 3J1I 3J1J 3J1K 3J1L
• EMDBエントリー: 5392
• 分子名称: Chaperonin alpha subunit (1 entity in total)
• 機能のキーワード: group ii chaperonin, chaperone
• 由来する生物種: Acidianus tengchongensis
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 1084847.13

構造登録者

Zhang, K.,Wang, L.,Liu, Y.X.,Wang, X.,Gao, B.,Hu, Z.J.,Ji, G.,Chan, K.Y.,Schulten, K.,Dong, Z.Y.,Sun, F. (登録日: 2012-02-06, 公開日: 2013-08-07, 最終更新日: 2024-02-21)

主引用文献

Zhang, K.,Wang, L.,Liu, Y.,Chan, K.Y.,Pang, X.,Schulten, K.,Dong, Z.,Sun, F.
Flexible interwoven termini determine the thermal stability of thermosomes.
Protein Cell, 4:432-444, 2013

PubMed Abstract: Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-β), also called thermosomes, from Acidianus tengchongensis and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.

PubMed: 23709365
DOI: 10.1007/s13238-013-3026-9

実験手法

ELECTRON MICROSCOPY (9.1 Å)