- EMDB-1202: An expanded protein folding cage in the GroEL-gp31 complex. -
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基本情報
登録情報
データベース: EMDB / ID: EMD-1202
タイトル
An expanded protein folding cage in the GroEL-gp31 complex.
マップデータ
GroEL-gp31-ADP 3D density map. The box size is 192,192,192 and the map is centred at 0,0,0.
試料
試料: GroEL-ADP-gp31
タンパク質・ペプチド: GroEL
タンパク質・ペプチド: gp31
リガンド: ADP
機能・相同性
機能・相同性情報
protein binding / GroEL-GroES complex / viral capsid assembly / 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 ...protein binding / GroEL-GroES complex / viral capsid assembly / 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 / identical protein binding / membrane / cytosol 類似検索 - 分子機能
ジャーナル: J Mol Biol / 年: 2006 タイトル: An expanded protein folding cage in the GroEL-gp31 complex. 著者: Daniel K Clare / Patrick J Bakkes / Harm van Heerikhuizen / Saskia M van der Vies / Helen R Saibil / 要旨: Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to ...Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to obtain three-dimensional structures of the E.coli chaperonin GroEL complexed with gp31, in the presence of both ATP and ADP. The GroEL-gp31-ADP map has a resolution of 8.2 A, which allows accurate fitting of the GroEL and gp31 crystal structures. Comparison of this fitted structure with that of the GroEL-GroES-ADP structure previously determined by cryo-electron microscopy shows that the folding cage is expanded. The enlarged volume for folding is consistent with the size of the bacteriophage coat protein gp23, which is the major substrate of GroEL-gp31 chaperonin complex. At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage.
凍結剤: ETHANE / チャンバー内湿度: 95 % / チャンバー内温度: 100 K / 装置: HOMEMADE PLUNGER / 詳細: Vitrification instrument: home made / Timed resolved state: Vitrified after 10 minute incubation 手法: The grids were bloted for 2-3 seconds and then left to equilibrate for 2-3 seconds and then plunged into liquid ethane
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電子顕微鏡法
顕微鏡
FEI TECNAI F20
温度
平均: 100 K
アライメント法
Legacy - 非点収差: objective lens astigmatism corrected at 150kX