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-Structure paper
タイトル | Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 114, Issue 31, Page 8259-8264, Year 2017 |
掲載日 | 2017年8月1日 |
![]() | Soung-Hun Roh / Corey F Hryc / Hyun-Hwan Jeong / Xue Fei / Joanita Jakana / George H Lorimer / Wah Chiu / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.5 Å |
構造データ | |
化合物 | ![]() ChemComp-HOH: |
由来 |
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![]() | CHAPERONE / GroEL / cryoEM / conformational heterogeneity. |