Pedersen P L, Ko Y H, Hong S
Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205-2185, USA.
J Bioenerg Biomembr. 2000 Aug;32(4):325-32. doi: 10.1023/a:1005594800983.
This introductory article briefly summarizes how our views about the structural features of ATP synthases (F0F1) have evolved over the past 30 years and also reviews some of our current views in the year 2000 about the structures of these remarkably unique enzyme complexes. Suffice it to say that as we approach the end of the first year of this new millinium, we can be conservatively confident that we have a reasonably good grasp of the overall "low-resolution" structural features of ATP synthases. Electron microscopy techniques, combined with the tools of biochemistry, molecular biology, and immunology, have played the leading role here by identifying the headpiece, basepiece, central stalk, side stalk, cap, and in the mitochondrial enzyme, the collar around the central stalk. We can be reasonably confident also that we have a fairly good grasp of much of the "high-resolution" structural features of both the F1 moiety comprised of fives subunit types (alpha, beta, gamma, delta, and epsilon) and parts of the F0 moiety comprised of either three (E. coli) or at least ten (mitochondria) subunit types. This information acquired in several different laboratories, either by X-ray crystallography or NMR spectroscopy, includes details about the active site and subunit relationships. Moreover, it is consistent with recently reported data that the F1 moiety may be an ATP driven motor, which, during ATP synthesis, is driven in reverse by the electrochemical proton gradient generated by the electron transport chain. The real structural challenges of the future are to acquire at high resolution "complete" ATP synthase complexes representative of different stages of the catalytic cycle during ATP synthesis and representative also of key regulatory states.
这篇介绍性文章简要总结了在过去30年里我们对ATP合酶（F0F1）结构特征的看法是如何演变的，同时也回顾了我们在2000年对这些极其独特的酶复合物结构的一些当前观点。可以说，在我们即将迈入新千年的第一年年底时，我们可以较为保守地确信，我们已经对ATP合酶的整体“低分辨率”结构特征有了相当不错的理解。电子显微镜技术与生物化学、分子生物学和免疫学工具相结合，通过识别头部、基部、中央轴、侧轴、帽以及在线粒体酶中围绕中央轴颈环，在此发挥了主导作用。我们也可以相当有信心地认为，我们对由五种亚基类型（α、β、γ、δ和ε）组成的F1部分以及由三种（大肠杆菌）或至少十种（线粒体）亚基类型组成的F0部分的许多“高分辨率”结构特征有了相当好的理解。通过X射线晶体学或核磁共振光谱在几个不同实验室获得的这些信息，包括有关活性位点和亚基关系的细节。此外，这与最近报道的数据一致，即F1部分可能是一个由ATP驱动的马达，在ATP合成过程中，它由电子传递链产生的电化学质子梯度反向驱动。未来真正的结构挑战是获得高分辨率的“完整”ATP合酶复合物，这些复合物代表ATP合成过程中催化循环的不同阶段，同时也代表关键的调节状态。
