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Structure paper

TitleStructural insights into thermophilic chaperonin complexes.
Journal, issue, pagesStructure, Year 2024
Publish dateMar 6, 2024
AuthorsZengwei Liao / Chai C Gopalasingam / Masafumi Kameya / Christoph Gerle / Hideki Shigematsu / Masaharu Ishii / Takatoshi Arakawa / Shinya Fushinobu /
PubMed AbstractGroup 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.
External linksStructure / PubMed:38492570
MethodsEM (single particle)
Resolution2.5 - 3.3 Å
Structure data

37850

8wu4

EMDB-37850, PDB-8wu4:
Cryo-EM structure of native H. thermoluteolus TH-1 GroEL
Method: EM (single particle) / Resolution: 3.3 Å

37853

8wuc

EMDB-37853, PDB-8wuc:
Cryo-EM structure of H. thermoluteolus GroEL-GroES2 football complex
Method: EM (single particle) / Resolution: 2.5 Å

37862

8wuw

EMDB-37862, PDB-8wuw:
Cryo-EM structure of H. thermophilus GroEL-GroES2 asymmetric football complex
Method: EM (single particle) / Resolution: 2.6 Å

37863

8wux

EMDB-37863, PDB-8wux:
Cryo-EM structure of H. thermophilus GroEL-GroES bullet complex
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-K:
Unknown entry

Source
  • hydrogenophilus thermoluteolus (bacteria)
  • hydrogenobacter thermophilus tk-6 (bacteria)
KeywordsCHAPERONE / Chaperonin / ATPase / protein folding

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