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牛线粒体F-ATP酶调节亚基IF(1)的结构。

The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase.

作者信息

Cabezón E, Runswick M J, Leslie A G, Walker J E

机构信息

The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.

出版信息

EMBO J. 2001 Dec 17;20(24):6990-6. doi: 10.1093/emboj/20.24.6990.

Abstract

In mitochondria, the hydrolytic activity of ATP synthase is regulated by an inhibitor protein, IF(1). Its binding to ATP synthase depends on pH, and below neutrality, IF(1) is dimeric and forms a stable complex with the enzyme. At higher pH values, IF(1) forms tetramers and is inactive. In the 2.2 A structure of the bovine IF(1) described here, the four monomers in the asymmetric unit are arranged as a dimer of dimers. Monomers form dimers via an antiparallel alpha-helical coiled coil in the C-terminal region. Dimers are associated into oligomers and form long fibres in the crystal lattice, via coiled-coil interactions in the N-terminal and inhibitory regions (residues 14-47). Therefore, tetramer formation masks the inhibitory region, preventing IF(1) binding to ATP synthase.

摘要

在线粒体中,ATP合酶的水解活性受抑制蛋白IF(1)调控。它与ATP合酶的结合取决于pH值,在中性pH以下,IF(1)呈二聚体形式,并与该酶形成稳定复合物。在较高pH值时,IF(1)形成四聚体且无活性。在此处描述的牛IF(1)的2.2埃结构中,不对称单元中的四个单体排列成二聚体的二聚体。单体通过C端区域的反平行α-螺旋卷曲螺旋形成二聚体。二聚体通过N端和抑制区域(第14至47位残基)中的卷曲螺旋相互作用聚合成寡聚体,并在晶格中形成长纤维。因此,四聚体的形成掩盖了抑制区域,阻止IF(1)与ATP合酶结合。

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