- EMDB-37853: Cryo-EM structure of H. thermoluteolus GroEL-GroES2 football complex -
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基本情報
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データベース: EMDB / ID: EMD-37853
タイトル
Cryo-EM structure of H. thermoluteolus GroEL-GroES2 football complex
マップデータ
試料
複合体: H. thermoluteolus GroEL-GroES2 football complex bound with ADP-Mg2+
複合体: H. thermoluteolus GroEL
タンパク質・ペプチド: Chaperonin GroEL
複合体: H. thermoluteolus GroES
タンパク質・ペプチド: Co-chaperonin GroES
リガンド: ADENOSINE-5'-DIPHOSPHATE
リガンド: MAGNESIUM ION
キーワード
Chaperone / Chaperonin / ATPase / protein folding
機能・相同性
機能・相同性情報
GroEL-GroES complex / chaperonin ATPase / mitochondrial unfolded protein response / protein import into mitochondrial intermembrane space / chaperone cofactor-dependent protein refolding / positive regulation of interferon-alpha production / protein folding chaperone / isomerase activity / ATP-dependent protein folding chaperone / positive regulation of interleukin-6 production ...GroEL-GroES complex / chaperonin ATPase / mitochondrial unfolded protein response / protein import into mitochondrial intermembrane space / chaperone cofactor-dependent protein refolding / positive regulation of interferon-alpha production / protein folding chaperone / isomerase activity / ATP-dependent protein folding chaperone / positive regulation of interleukin-6 production / positive regulation of type II interferon production / unfolded protein binding / positive regulation of T cell activation / protein-folding chaperone binding / response to heat / protein refolding / ATP binding / cytoplasm 類似検索 - 分子機能
ジャーナル: Structure / 年: 2024 タイトル: Structural insights into thermophilic chaperonin complexes. 著者: Zengwei Liao / Chai C Gopalasingam / Masafumi Kameya / Christoph Gerle / Hideki Shigematsu / Masaharu Ishii / Takatoshi Arakawa / Shinya Fushinobu / 要旨: Group I chaperonins are dual heptamer protein complexes that play significant roles in protein homeostasis. The structure and function of the Escherichia coli chaperonin are well characterized. ...Group I chaperonins are dual heptamer protein complexes that play significant roles in protein homeostasis. The structure and function of the Escherichia coli chaperonin are well characterized. However, the dynamic properties of chaperonins, such as large ATPase-dependent conformational changes by binding of lid-like co-chaperonin GroES, have made structural analyses challenging, and our understanding of these changes during the turnover of chaperonin complex formation is limited. In this study, we used single-particle cryogenic electron microscopy to investigate the structures of GroES-bound chaperonin complexes from the thermophilic hydrogen-oxidizing bacteria Hydrogenophilus thermoluteolus and Hydrogenobacter thermophilus in the presence of ATP and AMP-PNP. We captured the structure of an intermediate state chaperonin complex, designated as an asymmetric football-shaped complex, and performed analyses to decipher the dynamic structural variations. Our structural analyses of inter- and intra-subunit communications revealed a unique mechanism of complex formation through the binding of a second GroES to a bullet-shaped complex.
全体 : H. thermoluteolus GroEL-GroES2 football complex bound with ADP-Mg2+
全体
名称: H. thermoluteolus GroEL-GroES2 football complex bound with ADP-Mg2+
要素
複合体: H. thermoluteolus GroEL-GroES2 football complex bound with ADP-Mg2+
複合体: H. thermoluteolus GroEL
タンパク質・ペプチド: Chaperonin GroEL
複合体: H. thermoluteolus GroES
タンパク質・ペプチド: Co-chaperonin GroES
リガンド: ADENOSINE-5'-DIPHOSPHATE
リガンド: MAGNESIUM ION
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超分子 #1: H. thermoluteolus GroEL-GroES2 football complex bound with ADP-Mg2+
超分子
名称: H. thermoluteolus GroEL-GroES2 football complex bound with ADP-Mg2+ タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#2 詳細: 6.76 mg/mL native GroEL was mixed with 3.7 mg/mL recombinant GroES followed by addition of 2 mM ATP in imaging buffer supplemented by detergents (0.1% 3-((3-cholamidopropyl) dimethylammonio)- ...詳細: 6.76 mg/mL native GroEL was mixed with 3.7 mg/mL recombinant GroES followed by addition of 2 mM ATP in imaging buffer supplemented by detergents (0.1% 3-((3-cholamidopropyl) dimethylammonio)-1-propanesulfonate (CHAPS), 0.05% n-Octyl-beta-D-glucopyranoside)