Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.

Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.
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DOI:
10.1038/nsmb.2284
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发表时间:
2012-04-15
影响因子:
16.8
通讯作者:
Mueller, David M.
Mueller, David M.
中科院分区:
生物学1区
文献类型:
--
作者:
Symersky, Jindrich;Pagadala, Vijayakanth;Osowski, Daniel;Krah, Alexander;Meier, Thomas;Faraldo-Gomez, Jose D.;Mueller, David M.

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F1 Fo-ATP酶的质子孔由c-亚基环组成,其由质子向下扩散驱动旋转。C亚基中的必需羧酸侧链提供质子结合位点。在迄今为止报道的所有c环结构中,这些位点都处于封闭的离子锁定状态。给出了在pH8.3、6.1和5.5条件下测定的酿酒酵母c10环的结构,分辨率分别为2.0 μ m、2.5 μ m和2.0 μ m。这个线粒体C环的整体结构与已知的同系物相似,除了必需的羧酸盐Glu 59采用开放的延伸构象。分子动力学模拟表明,开放的基本羧酸盐的结晶缓冲液的两亲性的结果。我们认为这种新的结构代表了c亚基的功能开放形式,这有利于质子的装载和释放。
The proton pores of F1Fo-ATP synthases consist of a ring of c-subunits, which rotates driven by downhill proton diffusion. An essential carboxylate side chain in the c-subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are presented of the c10 ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologues, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c-subunit, which facilitates proton loading and release.
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