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Rotatory catalysis in V1-ATPase

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made with VMD

Living cells employ an intricate network of biochemical processes for the conversion of solar energy or nutrients into energy-rich Adenosine Tri Phosphate (ATP) molecules. From bacteria to fungi, plants, and animals, ATP serves as the universal energy currency of life, fueling the processes cells need to survive and function. Over the course of a day, an individual will typically use the equivalent of his or her bodyweight in ATP; however, the human body carries only a small amount of the molecule at any one time. That means cells must constantly recycle or replenish the ATP molecules, relying on a highly efficient motor protein called ATP synthase to do the job. Given its ubiquitous role in photosynthesis and respiration, efficiency of the ATP synthase motor has been a focus of intense biochemical investigations over the past three decades, which included Boyer and Walker's Nobel Prize-winning contributions in 1997. Yet, connection between the Chemistry of ATP dissociation and Physics of ATP synthase motor-action remained elusive. A recent study based on molecular dynamics simulations with NAMD reveals the working principles of V-type ATP synthase in atomic resolution. Swiveling motions in the protein ring were captured together with rubber band-like elasticity of the motor's central stalk. This swiveling motion of the ring when paired with the stalk absorbs about 75 percent of the energy released during ATP hydrolysis, showcasing a molecular design that underlies the molecular motor's remarkable energy-conversion efficiency. More on ATPase here and here.