Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8WUW

Cryo-EM structure of H. thermophilus GroEL-GroES2 asymmetric football complex

Summary for 8WUW
Entry DOI10.2210/pdb8wuw/pdb
Related8WU4 8WUC
EMDB information37850 37853 37862
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 chains28
Total formula weight949106.94
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

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon