Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy.

ABSTRACT: 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.

SUBMITTER: Zeng YC 

PROVIDER: S-EPMC7938637 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature