3CAU

D7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEM

3CAU の概要

• エントリーDOI: 10.2210/pdb3cau/pdb
• 関連するPDBエントリー: 3C9V
• EMDBエントリー: 5001
• 分子名称: 60 kDa chaperonin (1 entity in total)
• 機能のキーワード: groel, atp-binding, cell cycle, cell division, chaperone, nucleotide-binding, phosphoprotein
• 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: 774636.58

構造登録者

Ludtke, S.J.,Baker, M.L.,Chen, D.H.,Song, J.L.,Chuang, D.,Chiu, W. (登録日: 2008-02-20, 公開日: 2008-09-02, 最終更新日: 2024-02-21)

主引用文献

Ludtke, S.J.,Baker, M.L.,Chen, D.H.,Song, J.L.,Chuang, D.T.,Chiu, W.
De Novo Backbone Trace of GroEL from Single Particle Electron Cryomicroscopy.
Structure, 16:441-448, 2008

PubMed Abstract: In this work, we employ single-particle electron cryo-microscopy (cryo-EM) to reconstruct GroEL to approximately 4 A resolution with both D7 and C7 symmetry. Using a newly developed skeletonization algorithm and secondary structure element identification in combination with sequence-based secondary structure prediction, we demonstrate that it is possible to achieve a de novo Calpha trace directly from a cryo-EM reconstruction. The topology of our backbone trace is completely accurate, though subtle alterations illustrate significant differences from existing crystal structures. In the map with C7 symmetry, the seven monomers in each ring are identical; however, the subunits have a subtly different structure in each ring, particularly in the equatorial domain. These differences include an asymmetric salt bridge, density in the nucleotide-binding pocket of only one ring, and small shifts in alpha helix positions. This asymmetric conformation is different from previous asymmetric structures, including GroES-bound GroEL, and may represent a "primed state" in the chaperonin pathway.

PubMed: 18334219
DOI: 10.1016/j.str.2008.02.007

実験手法

ELECTRON MICROSCOPY (4.2 Å)