Today we know there are four different types of ATPases/ATP synthases that operate within biological membranes with the purpose of moving many different types of ions or molecules across the membranes. Some of these ions or molecules are transported into cells, some out of cells, and some in or out of organelles within cells. These ATPases/ATP synthases, which are made up of 8-16 subunits, span the biological world from bacteria to eukaryotic cells and have most simply and commonly known as “transport ATPases”. The price that each cell type pays for transport work is counted in molecules of hydrolyzed ATP, a metabolic currency that is itself regenerated by a transport ATPase working in reverse, i.e., the ATP synthase. In addition to being involved in many different types of biological/physiological processes, mutations in these proteins also account for a large number of diseases.
We have used 2D and 3D NMR spectroscopy to determine the solution structures of individual subunits of V-ATPases, A- and F-ATP synthases as well as their interaction epitopes. These structural features will be compared with our recently determined crystallographic structures. The purpose of the presentation is to provide a focused look at this important area of research that bears significance to cell physiology, biochemistry, immunology, nanotechnology, and medicine, including drug discovery.