Structure And Supramolecular Architecture Of Chloroplast Atp Synthase

The chloroplast FoF1 ATP synthase-a multi-subunit enzyme located in the plant thylakoid membrane-couples the electrochemical proton gradient built up by photosynthetic electron transport reactions to the synthesis of ATP. Synthesis of this universal cellular energy source in the extra-membranous F-1 module is driven by rotary motions in the FoF1 holoenzyme that are powered by proton transport across the membrane-embedded Fo-submodule. Our mechanistic understanding of the ATP synthase has tremendously benefited from detailed insights into the structure and supramolecular architecture of this marvelous molecular machine which have enormously grown in the last decades. This started with low-resolution electron microscopic images of the FoF1 complex, went on with atomic resolution structures of individual subunits or subcomplexes resolved by X-ray crystallography or nuclear magnetic resonance and eventually culminated in a high-resolution molecular model of the complete chloroplast FoF1 holoenzyme obtained by cryo-electron microscopy.