1SX3
GroEL14-(ATPgammaS)14
1SX3 の概要
エントリーDOI | 10.2210/pdb1sx3/pdb |
分子名称 | groEL protein, MAGNESIUM ION, POTASSIUM ION, ... (5 entities in total) |
機能のキーワード | groel, protein folding, molecular chaperone, chaperone |
由来する生物種 | Escherichia coli |
細胞内の位置 | Cytoplasm : P0A6F5 |
タンパク質・核酸の鎖数 | 14 |
化学式量合計 | 782172.08 |
構造登録者 | Chaudhry, C.,Horwich, A.L.,Brunger, A.T.,Adams, P.D. (登録日: 2004-03-30, 公開日: 2005-03-01, 最終更新日: 2024-02-14) |
主引用文献 | Chaudhry, C.,Horwich, A.L.,Brunger, A.T.,Adams, P.D. Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states. J.Mol.Biol., 342:229-245, 2004 Cited by PubMed Abstract: Large rigid-body domain movements are critical to GroEL-mediated protein folding, especially apical domain elevation and twist associated with the formation of a folding chamber upon binding ATP and co-chaperonin GroES. Here, we have modeled the anisotropic displacements of GroEL domains from various crystallized states, unliganded GroEL, ATPgammaS-bound, ADP-AlFx/GroES-bound, and ADP/GroES bound, using translation-libration-screw (TLS) analysis. Remarkably, the TLS results show that the inherent motions of unliganded GroEL, a polypeptide-accepting state, are biased along the transition pathway that leads to the folding-active state. In the ADP-AlFx/GroES-bound folding-active state the dynamic modes of the apical domains become reoriented and coupled to the motions of bound GroES. The ADP/GroES complex exhibits these same motions, but they are increased in magnitude, potentially reflecting the decreased stability of the complex after nucleotide hydrolysis. Our results have allowed the visualization of the anisotropic molecular motions that link the static conformations previously observed by X-ray crystallography. Application of the same analyses to other macromolecules where rigid body motions occur may give insight into the large scale dynamics critical for function and thus has the potential to extend our fundamental understanding of molecular machines. PubMed: 15313620DOI: 10.1016/j.jmb.2004.07.015 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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