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Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo‐electron microscopy
Author(s) -
Zeng Yi Cheng,
Sobti Meghna,
Stewart Alastair G.
Publication year - 2021
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x21002223
Subject(s) - sulfolobus solfataricus , chaperonin , thermophile , archaea , sulfolobus , folding (dsp implementation) , cryo electron microscopy , protein folding , crystallography , electron microscope , chemistry , biochemistry , biology , biophysics , enzyme , physics , gene , engineering , electrical engineering , optics
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.