Structure, rotation and regulation of ATP synthase(FoF1)

ATP合酶(FoF1)的结构、旋转和调控

• 批准号: 18107004
• 负责人: YOSHIDA Masasuke
• 金额: $ 71.22万
• 依托单位: Kyoto Sangyo University (2010)Tokyo Institute of Technology (2006-2009)
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (S)
• 财政年份: 2006
• 资助国家: 日本
• 起止时间: 2006 至 2010
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-18107004/
• 关键词: ATP合成; ATP合成酵素; F_oF_1; モータータンパク質; 生体エネルギー; FoF1; F1; モーター; F0F1; 回転モーター; ATP; 結晶解析; プロトン; εサブユニット; FoFl; Fl; Fo; 分子モーター

We made F_1-ATPases containing one or two mutant. β subunits that have the altered catalytic kinetics. The analysis of their asymmetric stepwise rotations reveal that, when watching one. β subunit in F_1-ATPase, it binds ATP at 0°, cleaves ATP after～ 200°rotation, and undergoes the final catalytic event, presumably the product release, after～ 320°rotation. Three. β subunits carry out this cycle at 120°difference like "trolling a tune" and their cyclic inter-domain bending motions would induce the rotation of γ subunit.Rotation of the central shaft γ subunit in a molecular motor F_1-ATPase is assumed to correlate with and probably be driven by domain motions of the three catalytic. β subunits. Here we observe directly these. β motions through an attached fluorophore, concomitantly with 80 degrees and 40 degrees substep rotations of γ in the same single molecules. We show the sequence of conformations that each β subunit undergoes in three-step bending, an approximately 40 degrees counterclockwise turn followed by two approximately 20 degrees clockwise turns, occurring in synchronization with two substep rotations of γ. The results indicate that most previous crystal structures mimic the conformational set of three β subunits in the catalytic dwells. Moreover, a previously undescribed set of β conformations, open, closed and partially closed, is revealed in the ATP-waiting dwells. The present study thus bridges the gap between the chemical and mechanical steps in F_1-ATPase.

我们制作了含有一个或两个突变体的F_1-ATP酶。具有改变催化动力学的β亚基。对它们的不对称逐步旋转的分析表明，观看时。 β亚基在F_1-ATPase中，它在旋转〜200°后的0°时结合ATP，裂解ATP，并经历了〜320°旋转后的最终催化事件，大概是产物释放。三。 β亚基在120°的差异下进行此周期，例如“ troll tune tune”，它们的环状域弯曲运动会诱导γ亚基的旋转。中央轴γ亚基在分子运动F_1-ATPase中的旋转，假定与三个三型尾部运动的旋转相关性并可能与三型尾型相关。 β亚基。在这里，我们直接观察到这些。 β通过附着的荧光团的运动，同时在同一单分子中以80度和40度的取代γ旋转。我们显示了每个β亚基在三步弯曲中经历的构象顺序，逆时针逆时针弯曲大约40度，然后是两个大约20度的顺时针转弯，与两个γ的取代旋转同步发生。结果表明，大多数先前的晶体结构都模仿了催化住宅中三个β亚基的构象集。此外，在ATP等待中揭示了一组未描述的β构象，即开放，闭合和部分闭合。因此，本研究弥合了F_1-ATPase中化学和机械步骤之间的差距。

项目成果

Cooperative three-step motions in catalytic subunits of F1-ATPase correlate with 80 degrees and 40 degrees substep rotations

F1-ATPase 催化亚基中的协作三步运动与 80 度和 40 度分步旋转相关

• 发表时间: 2008
• 期刊: Nat Struct Mol Biol 15
• 作者: Masaike T;Koyama-Horibe F;Oiwa K;Yoshida M;Nishizaka T.
• 通讯作者: Nishizaka T.

Regulatory transition of subunit epsilon in ATP synthase from Bacillus PS3

芽孢杆菌 PS3 ATP 合酶亚基 epsilon 的调控转变

• 发表时间: 2008
• 作者: B. A. Feniouk;T. Suzuki;M. Yoshida
• 通讯作者: M. Yoshida

Axle-less Fl-ATPase rotates in the correct direction.

无轴 Fl-ATP 酶以正确的方向旋转。

• 发表时间: 2008
• 期刊: Science. 319
• 作者: Furuike S;Hossain MD;MakiY;Adachi K;Suzuki T;Kohori A;Itoh H;Yoshida M;Kinosita K Jr.
• 通讯作者: Kinosita K Jr.

Temperature-sensitive reaction intermediate of F1-ATPase.

• DOI: 10.1038/sj.embor.7401135
• 发表时间: 2008-01
• 期刊: EMBO REPORTS
• 影响因子: 7.7
• 作者: Watanabe, Rikiya;Iino, Ryota;Shimabukuro, Katsuya;Yoshida, Masasuke;Noji, Hiroyuki
• 通讯作者: Noji, Hiroyuki

Mechanism and regulation of F_oF_<1-> motor

F_oF_<1->电机的机理和调节

• 发表时间: 2008
• 作者: Fukuzawa;N.;M. Yoshida
• 通讯作者: M. Yoshida