Single particle cryo-EM of H. thermoluteolus chaperonin complex
Ontology highlight
ABSTRACT:
SUBMITTER: Zengwei Liao
PROVIDER: EMPIAR-11900 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural insights into thermophilic chaperonin complexes.
Liao Zengwei Z Gopalasingam Chai C CC Kameya Masafumi M Gerle Christoph C Shigematsu Hideki H Ishii Masaharu M Arakawa Takatoshi T Fushinobu Shinya S
Structure (London, England : 1993) 20240315 6
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, ...[more]
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