5W0S

GroEL using cryoEM

5W0S の概要

• エントリーDOI: 10.2210/pdb5w0s/pdb
• EMDBエントリー: 8750
• 分子名称: 60 kDa chaperonin (2 entities in total)
• 機能のキーワード: groel, cryoem, conformational heterogeneity., chaperone
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 772072.28

構造登録者

Roh, S.H.,Chiu, W. (登録日: 2017-05-31, 公開日: 2017-08-09, 最終更新日: 2024-03-13)

主引用文献

Roh, S.H.,Hryc, C.F.,Jeong, H.H.,Fei, X.,Jakana, J.,Lorimer, G.H.,Chiu, W.
Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM.
Proc. Natl. Acad. Sci. U.S.A., 114:8259-8264, 2017

PubMed Abstract: Single-particle electron cryo-microscopy (cryo-EM) is an emerging tool for resolving structures of conformationally heterogeneous particles; however, each structure is derived from an average of many particles with presumed identical conformations. We used a 3.5-Å cryo-EM reconstruction with imposed D7 symmetry to further analyze structural heterogeneity among chemically identical subunits in each GroEL oligomer. Focused classification of the 14 subunits in each oligomer revealed three dominant classes of subunit conformations. Each class resembled a distinct GroEL crystal structure in the Protein Data Bank. The conformational differences stem from the orientations of the apical domain. We mapped each conformation class to its subunit locations within each GroEL oligomer in our dataset. The spatial distributions of each conformation class differed among oligomers, and most oligomers contained 10-12 subunits of the three dominant conformation classes. Adjacent subunits were found to more likely assume the same conformation class, suggesting correlation among subunits in the oligomer. This study demonstrates the utility of cryo-EM in revealing structure dynamics within a single protein oligomer.

PubMed: 28710336
DOI: 10.1073/pnas.1704725114

実験手法

ELECTRON MICROSCOPY (3.5 Å)