Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo‐electron microscopy. Issue 3 (8th March 2021)

• Record Type: Journal Article
• Authors: Zeng, Yi Cheng; Sobti, Meghna; Stewart, Alastair G.
• Is Part Of: Acta crystallographica. Volume 77:Issue 3(2021)
• Page Start: 79
• Page End: 84
• Publication Date: 2021-03-08
• Subjects: chaperonins -- cryo‐electron microscopy; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X21002223
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The isolated complex of the TF55β chaperonin from the thermophilic archaeon Sulfolobus solfataricus are reported. The structures of nucleotide‐bound complexes of TF55β obtained at 3.6–4.2 Å resolution using cryo‐EM reveal an open conformation. 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.