4PKO
Crystal structure of the Football-shaped GroEL-GroES2-(ADPBeFx)14 complex
4PKO の概要
| エントリーDOI | 10.2210/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: 25136110DOI: 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) |
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