- EMDB-13308: Cryo-EM structure of the GroEL-GroES complex with ADP bound to bo... -
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基本情報
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データベース: EMDB / ID: EMD-13308
タイトル
Cryo-EM structure of the GroEL-GroES complex with ADP bound to both rings ("tight" conformation).
マップデータ
Locally sharpened C7 map of "tight" conformation of the GroEL-GroES complex. ADP bound to both rings.
試料
複合体: ADP-bound GroEL-GroES complex
タンパク質・ペプチド: 10 kDa chaperonin
タンパク質・ペプチド: 60 kDa chaperonin
リガンド: ADENOSINE-5'-DIPHOSPHATE
リガンド: MAGNESIUM ION
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 / virion assembly / chaperone cofactor-dependent protein refolding / positive regulation of interferon-alpha production / protein folding chaperone / isomerase activity / ATP-dependent protein folding chaperone ...GroEL-GroES complex / chaperonin ATPase / mitochondrial unfolded protein response / protein import into mitochondrial intermembrane space / virion assembly / chaperone cofactor-dependent protein refolding / positive regulation of interferon-alpha production / protein folding chaperone / isomerase activity / ATP-dependent protein folding chaperone / response to radiation / positive regulation of interleukin-6 production / positive regulation of type II interferon production / unfolded protein binding / positive regulation of T cell activation / protein folding / protein-folding chaperone binding / response to heat / protein refolding / magnesium ion binding / ATP hydrolysis activity / ATP binding / membrane / identical protein binding / metal ion binding / cytosol 類似検索 - 分子機能
ジャーナル: Sci Rep / 年: 2021 タイトル: Novel cryo-EM structure of an ADP-bound GroEL-GroES complex. 著者: Sofia S Kudryavtseva / Evgeny B Pichkur / Igor A Yaroshevich / Aleksandra A Mamchur / Irina S Panina / Andrei V Moiseenko / Olga S Sokolova / Vladimir I Muronetz / Tatiana B Stanishneva-Konovalova / 要旨: The GroEL-GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate ...The GroEL-GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural methods helped to reveal several conformational states and provide more information about the chaperonin functional cycle. Here, using cryo-EM we resolved two nucleotide-bound structures of the bullet-shaped GroEL-GroES complex at 3.4 Å resolution. The main difference between them is the relative orientation of their apical domains. Both structures contain nucleotides in cis and trans GroEL rings; in contrast to previously reported bullet-shaped complexes where nucleotides were only present in the cis ring. Our results suggest that the bound nucleotides correspond to ADP, and that such a state appears at low ATP:ADP ratios.