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8WUX

Cryo-EM structure of H. thermophilus GroEL-GroES bullet complex

Summary for 8WUX
Entry DOI10.2210/pdb8wux/pdb
Related8WU4 8WUC 8WUW
EMDB information37850 37853 37862 37863
DescriptorChaperonin GroEL, Co-chaperonin GroES, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordschaperone, chaperonin, atpase, protein folding
Biological sourceHydrogenobacter thermophilus TK-6
More
Total number of polymer chains21
Total formula weight873194.34
Authors
Liao, Z.,Gopalasingam, C.C.,Kameya, M.,Gerle, C.,Shigematsu, H.,Ishii, M.,Arakawa, T.,Fushinobu, S. (deposition date: 2023-10-21, release date: 2024-03-27, Last modification date: 2024-06-19)
Primary citationLiao, Z.,Gopalasingam, C.C.,Kameya, M.,Gerle, C.,Shigematsu, H.,Ishii, M.,Arakawa, T.,Fushinobu, S.
Structural insights into thermophilic chaperonin complexes.
Structure, 32:679-689.e4, 2024
Cited by
PubMed Abstract: 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.
PubMed: 38492570
DOI: 10.1016/j.str.2024.02.012
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.6 Å)
Structure validation

226707

건을2024-10-30부터공개중

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