Gibbons C, Montgomery M G, Leslie A G, Walker J E
The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.
Nat Struct Biol. 2000 Nov;7(11):1055-61. doi: 10.1038/80981.
The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The gamma subunit penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. In other crystals of F(1)-ATPase, the protrusion was disordered, but with crystals of F(1)-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (alpha beta)(3) domain.
线粒体酶中由γ、δ和ε亚基组成的ATP合酶中央轴是该酶催化机制中的关键旋转元件。γ亚基穿透催化性（αβ）3结构域并在其下方突出，与膜中驱动ATP合成过程中轴旋转的c亚基环相互作用。在F1-ATP酶的其他晶体中，突出部分无序，但在用二环己基碳二亚胺抑制的F1-ATP酶晶体中，完整结构得以揭示。δ和ε亚基与γ亚基中的Rossmann折叠相互作用，形成一个“脚”。在ATP合酶中，这个“脚”与c环相互作用，并将跨膜质子动力与（αβ）3结构域中的催化作用耦合起来。
