The structure of bovine F1-ATPase in complex with its regulatory protein IF1
The structure of bovine F1-ATPase in complex with its regulatory protein IF1
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DOI：
10.1038/nsb966
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发表时间：
2003-09-01
期刊：
影响因子：
--
通讯作者：
Walker, JE
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文献类型：
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作者：
Cabezón, E;Montgomery, MG;Walker, JE
在线粒体中，ATP合酶的水解活性被抑制蛋白IF 1阻止。活性牛蛋白（84个氨基酸）是α-螺旋二聚体，单体通过由残基49-81组成的反平行α-螺旋卷曲螺旋缔合。活性二聚体中的N-末端抑制序列在ATP存在下与两个F-1-ATP酶结合。在2.8埃分辨率下的F-1-IF 1复合物的晶体结构中，IF 1的残基1-37结合在F-1-ATP酶的α（DP）-β（DP）界面中，并且还接触中心γ亚基。相对于先前的结构，抑制剂打开α（DP）和β（DP）亚基之间的催化界面。在β（DP）亚基的催化位点存在ATP意味着抑制状态代表酶催化途径上的预水解步骤。
In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1. The active bovine protein (84 amino acids) is alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 49-81. The N-terminal inhibitory sequences in the active dimer bind to two F-1-ATPases in the presence of ATP. In the crystal structure of the F-1-IF1 complex at 2.8 Angstrom resolution, residues 1-37 of IF1 bind in the alpha(DP)-beta(DP) interface of F-1-ATPase, and also contact the central gamma subunit. The inhibitor opens the catalytic interface between the alpha(DP) and beta(DP) subunits relative to previous structures. The presence of ATP in the catalytic site of the beta(DP) subunit implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.