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4PKO

Crystal structure of the Football-shaped GroEL-GroES2-(ADPBeFx)14 complex

4PKO の概要
エントリーDOI10.2210/pdb4pko/pdb
関連するPDBエントリー4PKN
分子名称60 kDa chaperonin, 10 kDa chaperonin, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
機能のキーワードchaperonin, protein encapsulation, groel-groes2 complex, protein binding
由来する生物種Escherichia coli
詳細
細胞内の位置Cytoplasm (By similarity): Q548M1 Q7BGE6
タンパク質・核酸の鎖数28
化学式量合計956889.64
構造登録者
Fei, X.,Ye, X.,Laronde-Leblanc, N.,Lorimer, G.H. (登録日: 2014-05-15, 公開日: 2014-08-20, 最終更新日: 2024-10-09)
主引用文献Fei, X.,Ye, X.,LaRonde, N.A.,Lorimer, G.H.
Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form.
Proc.Natl.Acad.Sci.USA, 111:12775-12780, 2014
Cited by
PubMed Abstract: The GroE chaperonins assist substrate protein (SP) folding by cycling through several conformational states. With each cycle the SP is, in turn, captured, unfolded, briefly encapsulated (t1/2 ∼ 1 s), and released by the chaperonin complex. The protein-folding functional form is the US-football-shaped GroEL:GroES2 complex. We report structures of two such "football" complexes to ∼ 3.7-Å resolution; one is empty whereas the other contains encapsulated SP in both chambers. Although encapsulated SP is not visible on the electron density map, using calibrated FRET and order-of-addition experiments we show that owing to SP-catalyzed ADP/ATP exchange both chambers of the football complex encapsulate SP efficiently only if the binding of SP precedes that of ATP. The two rings of GroEL thus behave as a parallel processing machine, rather than functioning alternately. Compared with the bullet-shaped GroEL:GroES1 complex, the GroEL:GroES2 football complex differs conformationally at the GroEL-GroES interface and also at the interface between the two GroEL rings. We propose that the electrostatic interactions between the ε-NH(3+) of K105 of helix D in one ring with the negatively charged carboxyl oxygen of A109 at the carboxyl end of helix D of the other ring provide the structural basis for negative inter-ring cooperativity.
PubMed: 25136110
DOI: 10.1073/pnas.1412922111
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.84 Å)
構造検証レポート
Validation report summary of 4pko
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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