The synthesis of ATP, life's 'universal energy currency', is the most
prevalent chemical reaction in biological systems, and is responsible for
fueling nearly all cellular processes, from nerve impulse propagation to DNA
synthesis. ATP synthases, the family of enzymes that carry out this endless
task, are nearly as ubiquitous as the energy-laden molecule they are
responsible for making. The F-type ATP synthase (F-ATPase) is found in every
domain of life, and is believed to predate the divergence of these lineages
over 1.5 billion years ago. These enzymes have therefore facilitated the
survival of organisms in a wide range of habitats, ranging from the deep-sea
thermal vents to the human intestine. In this review, we present an overview of
the current knowledge of the structure and function of F-type ATPases,
highlighting several adaptations that have been characterized across taxa. We
emphasize the importance of studying these features within the context of the
enzyme's particular lipid environment: Just as the interactions between an
organism and its physical environment shape its evolutionary trajectory,
ATPases are impacted by the membranes within which they reside. We argue that a
comprehensive understanding of the structure, function, and evolution of
membrane proteins -- including ATP synthase -- requires such an integrative
approach.Comment: Review article; 29 pages, 6 figures/1 tabl