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-Structure paper
タイトル | Structural insights into thermophilic chaperonin complexes. |
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ジャーナル・号・ページ | Structure, Vol. 32, Issue 6, Page 679-689.e4, Year 2024 |
掲載日 | 2024年6月6日 |
著者 | Zengwei Liao / Chai C Gopalasingam / Masafumi Kameya / Christoph Gerle / Hideki Shigematsu / Masaharu Ishii / Takatoshi Arakawa / Shinya Fushinobu / |
PubMed 要旨 | Group I chaperonins are dual heptamer protein complexes that play significant roles in protein homeostasis. The structure and function of the Escherichia coli chaperonin are well characterized. ...Group I chaperonins are dual heptamer protein complexes that play significant roles in protein homeostasis. The structure and function of the Escherichia coli chaperonin are well characterized. However, the dynamic properties of chaperonins, such as large ATPase-dependent conformational changes by binding of lid-like co-chaperonin GroES, have made structural analyses challenging, and our understanding of these changes during the turnover of chaperonin complex formation is limited. In this study, we used single-particle cryogenic electron microscopy to investigate the structures of GroES-bound chaperonin complexes from the thermophilic hydrogen-oxidizing bacteria Hydrogenophilus thermoluteolus and Hydrogenobacter thermophilus in the presence of ATP and AMP-PNP. We captured the structure of an intermediate state chaperonin complex, designated as an asymmetric football-shaped complex, and performed analyses to decipher the dynamic structural variations. Our structural analyses of inter- and intra-subunit communications revealed a unique mechanism of complex formation through the binding of a second GroES to a bullet-shaped complex. |
リンク | Structure / PubMed:38492570 |
手法 | EM (単粒子) |
解像度 | 2.5 - 3.3 Å |
構造データ | EMDB-37850, PDB-8wu4: EMDB-37853, PDB-8wuc: EMDB-37862, PDB-8wuw: EMDB-37863, PDB-8wux: |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-ANP: ChemComp-K: |
由来 |
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キーワード | CHAPERONE / Chaperonin / ATPase / protein folding |