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本文引用的文献

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Methods used in the structure determination of bovine mitochondrial F1 ATPase.用于牛线粒体F1 ATP合酶结构测定的方法。
Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):30-42. doi: 10.1107/S0907444995008754.
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The CCP4 suite: programs for protein crystallography.CCP4软件包：用于蛋白质晶体学的程序。
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A NATURALLY OCCURRING INHIBITOR OF MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE.一种天然存在的线粒体腺苷三磷酸酶抑制剂。
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Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae.酿酒酵母V型ATP酶调节亚基H的晶体结构
Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7134-9. doi: 10.1073/pnas.131192798.
6
Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme.细菌F1F0 ATP合酶中ε亚基的大构象变化提供了一种棘轮作用，以调节这种旋转马达酶。
Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6560-4. doi: 10.1073/pnas.111128098. Epub 2001 May 29.
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The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways.Arfaptin介导的Rac与Arf信号通路间相互作用的结构基础。
Nature. 2001 May 10;411(6834):215-9. doi: 10.1038/35075620.
8
Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.来自牛IF(1)的C末端卷曲螺旋结构域的溶液结构：F(1)ATP酶的抑制蛋白
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9
Socket: a program for identifying and analysing coiled-coil motifs within protein structures.Socket：一个用于识别和分析蛋白质结构中卷曲螺旋基序的程序。
J Mol Biol. 2001 Apr 13;307(5):1427-50. doi: 10.1006/jmbi.2001.4545.
10
The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.牛F1 - ATP合酶中中央柄在2.4埃分辨率下的结构。
Nat Struct Biol. 2000 Nov;7(11):1055-61. doi: 10.1038/80981.

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.

DOI:10.1093/emboj/20.24.6990
PMID:11742976
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC125800/
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。