大鼠肝脏F1-ATP酶的2.8埃结构：ATP合成/水解关键中间体的构型
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis.
作者信息
Bianchet M A, Hullihen J, Pedersen P L, Amzel L M
机构信息
Department of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.
出版信息
Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11065-70. doi: 10.1073/pnas.95.19.11065.
Abstract
During mitochondrial ATP synthesis, F1-ATPase-the portion of the ATP 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 F1-ATPase, determined to 2.8-A 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 F1 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.
摘要
在线粒体ATP合成过程中，F1-ATP酶（ATP合酶中包含催化和调节性核苷酸结合位点的部分）会经历一系列协同的构象变化，这些变化将质子转运与细胞功能所需的高水平ATP合成相偶联。在生理浓度核苷酸存在下，大鼠肝脏F1-ATP酶的结构分辨率达到2.8埃，所有三个β亚基均含有结合的核苷酸并采用相似的构象。该结构提供了定义反应途径中所有中间体所需的F1缺失构型。结合此结构提示了一种ATP合成/水解机制，其中具有三个结合核苷酸的酶构型起着至关重要的作用。
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