Structural analysis of the Sulfolobus solfataricus TF55 β chaperonin by cryo-electron microscopy

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 (TF55 β ) were determined to 3.6 – 4.2   Å resolution. The structures of the TF55 β 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.

Source: Acta Crystallographica Section F - March 3, 2021 Category: Biochemistry Authors: Zeng, Y.C. Sobti, M. Stewart, A.G. Tags: chaperonins cryo-electron microscopy research communications Source Type: research