- EMDB-21211: Cryo-EM structure of a segment of the TF55 (beta-only) filament f... -
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基本情報
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データベース: EMDB / ID: EMD-21211
タイトル
Cryo-EM structure of a segment of the TF55 (beta-only) filament from S. solfataricus
マップデータ
TF55 beta segment of filament, D9 symmetric
試料
複合体: Octadecameric complex of TF55 chaperonin beta subunit
機能・相同性
機能・相同性情報
ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / ATP hydrolysis activity / ATP binding / identical protein binding 類似検索 - 分子機能
National Health and Medical Research Council (NHMRC, Australia)
APP1159347
オーストラリア
National Health and Medical Research Council (NHMRC, Australia)
APP1146403
オーストラリア
引用
ジャーナル: Acta Crystallogr F Struct Biol Commun / 年: 2021 タイトル: Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy. 著者: Yi Cheng Zeng / Meghna Sobti / Alastair G Stewart / 要旨: 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.