research communications
Chaperonins are biomolecular complexes that assist in protein folding. Thermophilic factor 55 (TF55) is a group II chaperonin found in the archaeal genus Sulfolobus that has α, β and γ subunits. Using cryo-electron microscopy, structures of the β-only complex of S. solfataricus TF55 (TF55β) were determined to 3.6–4.2 Å resolution. The structures of the TF55β complexes formed in the presence of ADP or ATP highlighted an open state in which nucleotide exchange can occur before progressing in the refolding cycle.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2053230X21002223/aq5008sup1.pdf |
EMDB references: TF55β, complex with ATP, EMD-22186; complex with ATP, EMD-22187
PDB references: TF55β, complex with ADP, 6xhi; complex with ATP, 6xhj