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1SX3

GroEL14-(ATPgammaS)14

1SX3 の概要
エントリーDOI10.2210/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: 15313620
DOI: 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)
構造検証レポート
Validation report summary of 1sx3
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2024-10-30に公開中

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