+Search query
-Structure paper
Title | Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy. |
---|---|
Journal, issue, pages | Acta Crystallogr F Struct Biol Commun, Vol. 77, Issue Pt 3, Page 79-84, Year 2021 |
Publish date | Mar 1, 2021 |
Authors | Yi Cheng Zeng / Meghna Sobti / Alastair G Stewart / |
PubMed 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. ...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. |
External links | Acta Crystallogr F Struct Biol Commun / PubMed:33682792 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.62 - 5.22 Å |
Structure data | EMDB-21211: EMDB-22186, PDB-6xhi: EMDB-22187, PDB-6xhj: |
Chemicals | ChemComp-ADP: ChemComp-MG: ChemComp-ATP: |
Source |
|
Keywords | CHAPERONE / Chaperonin / Complex |