- EMDB-21211: Cryo-EM structure of a segment of the TF55 (beta-only) filament f... -
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Basic information
Entry
Database: EMDB / ID: EMD-21211
Title
Cryo-EM structure of a segment of the TF55 (beta-only) filament from S. solfataricus
Map data
TF55 beta segment of filament, D9 symmetric
Sample
Complex: Octadecameric complex of TF55 chaperonin beta subunit
Function / homology
Function and homology information
chaperonin-containing T-complex / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / ATP hydrolysis activity / ATP binding / identical protein binding Similarity search - Function
National Health and Medical Research Council (NHMRC, Australia)
APP1159347
Australia
National Health and Medical Research Council (NHMRC, Australia)
APP1146403
Australia
Citation
Journal: Acta Crystallogr F Struct Biol Commun / Year: 2021 Title: Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy. Authors: Yi Cheng Zeng / Meghna Sobti / Alastair G Stewart / 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.
History
Deposition
Jan 12, 2020
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Header (metadata) release
Jan 29, 2020
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Map release
Mar 24, 2021
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Update
Oct 6, 2021
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Current status
Oct 6, 2021
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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