- EMDB-37863: Cryo-EM structure of H. thermophilus GroEL-GroES bullet complex -
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データベース: EMDB / ID: EMD-37863
タイトル
Cryo-EM structure of H. thermophilus GroEL-GroES bullet complex
マップデータ
試料
複合体: H. thermophilus GroEL-GroES bullet complex
複合体: chaperonin GroEL
タンパク質・ペプチド: Chaperonin GroEL
複合体: co-chaperonin GroES
タンパク質・ペプチド: Co-chaperonin GroES
リガンド: MAGNESIUM ION
リガンド: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
リガンド: POTASSIUM 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 / metal ion 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.