7PBX

Cryo-EM structure of the GroEL-GroES complex with ADP bound to both rings ("tight" conformation).

これはPDB形式変換不可エントリーです。

7PBX の概要

• エントリーDOI: 10.2210/pdb7pbx/pdb
• EMDBエントリー: 13308
• 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: cryo-em, chaperonin, groel, groel-groes, chaperone
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 852209.12

構造登録者

Pichkur, E.B.,Stanishneva-Konovalova, T.B. (登録日: 2021-08-02, 公開日: 2021-11-24, 最終更新日: 2024-07-17)

主引用文献

Kudryavtseva, S.S.,Pichkur, E.B.,Yaroshevich, I.A.,Mamchur, A.A.,Panina, I.S.,Moiseenko, A.V.,Sokolova, O.S.,Muronetz, V.I.,Stanishneva-Konovalova, T.B.
Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.
Sci Rep, 11:18241-18241, 2021

PubMed Abstract: The GroEL-GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural methods helped to reveal several conformational states and provide more information about the chaperonin functional cycle. Here, using cryo-EM we resolved two nucleotide-bound structures of the bullet-shaped GroEL-GroES complex at 3.4 Å resolution. The main difference between them is the relative orientation of their apical domains. Both structures contain nucleotides in cis and trans GroEL rings; in contrast to previously reported bullet-shaped complexes where nucleotides were only present in the cis ring. Our results suggest that the bound nucleotides correspond to ADP, and that such a state appears at low ATP:ADP ratios.

PubMed: 34521893
DOI: 10.1038/s41598-021-97657-x

実験手法

ELECTRON MICROSCOPY (3.43 Å)