8WU4
Cryo-EM structure of native H. thermoluteolus TH-1 GroEL
Summary for 8WU4
| Entry DOI | 10.2210/pdb8wu4/pdb |
| EMDB information | 37850 |
| Descriptor | Chaperonin GroEL (1 entity in total) |
| Functional Keywords | chaperone, chaperonin, atpase, protein folding |
| Biological source | Hydrogenophilus thermoluteolus |
| Total number of polymer chains | 14 |
| Total formula weight | 781718.98 |
| Authors | Liao, Z.,Gopalasingam, C.C.,Kameya, M.,Gerle, C.,Shigematsu, H.,Ishii, M.,Arakawa, T.,Fushinobu, S. (deposition date: 2023-10-20, release date: 2024-03-27, Last modification date: 2024-06-19) |
| Primary citation | Liao, 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: 38492570DOI: 10.1016/j.str.2024.02.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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