%0 Journal Article
%T An ATP "Synthase" Derived from a Single Structural Domain of Bacterial Histidine Kinase.
%A Ji S
%A Zhou Y
%A Chen J
%A Yang M
%A Li C
%A Liu M
%A Liu Y
%A Jiang L
%J Angew Chem Int Ed Engl
%V 63
%N 13
%D 2024 03 22
%M 38311597
%F 16.823
%R 10.1002/anie.202318503
%X ATP (adenosine triphosphate) is a vital energy source for living organisms, and its biosynthesis and precise concentration regulation often depend on macromolecular machinery composed of protein complexes or complicated multidomain proteins. We have identified a single-domain protein HK853CA derived from bacterial histidine kinases (HK) that can catalyze ATP synthesis efficiently. Here, we explored the reaction mechanism and multiple factors that influence this catalysis through a combination of experimental techniques and molecular simulations. Moreover, we optimized its enzymatic activity and applied it as an ATP replenishment machinery to other ATP-dependent systems. Our results broaden the understanding of ATP biosynthesis and show that the single CA domain can be applied as a new biomolecular catalyst used for ATP supply.