The 2.8-Å structure of rat liver F1-ATPase:: Configuration of a critical intermediate in ATP synthesis/hydrolysis
The 2.8-Å structure of rat liver F1-ATPase:: Configuration of a critical intermediate in ATP synthesis/hydrolysis
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DOI：
10.1073/pnas.95.19.11065
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发表时间：
1998-09-15
影响因子：
11.1
通讯作者：
Amzel, LM
中科院分区：
文献类型：
--
作者：
Bianchet, MA;Hullihen, J;Amzel, LM
在线粒体ATP合成过程中，F-1-ATP酶-ITP合酶的一部分，包含催化和调节核苷酸结合位点-经历了一系列协同的构象变化，将质子易位与细胞功能所需的高水平ATP的合成偶联。在大鼠肝脏F-1-ATP酶的结构中，在存在生理浓度的核苷酸的情况下测定到2.8埃分辨率，所有三个β亚基都含有结合的核苷酸并采用相似的构象。这种结构提供了定义反应途径中所有中间体所必需的F-1的缺失构型。该结构的引入表明了ATP合成/水解的机制，其中具有三个结合核苷酸的酶的构型起着至关重要的作用。
During mitochondrial ATP synthesis, F-1-ATPase-the portion of the;ITP synthase that contains the catalytic and regulatory nucleotide binding sites-undergoes a series of concerted conformational changes that couple proton translocation to the synthesis of the high levels of ATP required for cellular function. In the structure of the rat liver F-1-ATPase, determined to 2.8-Angstrom resolution in the presence of physiological concentrations of nucleotides, all three beta subunits contain bound nucleotide and adopt similar conformations. This structure provides the missing configuration of F-1 necessary to define all intermediates in the reaction pathway. Incorporation of this structure suggests a mechanism of ATP synthesis/hydrolysis in which configurations of the enzyme with three bound nucleotides play an essential role.