Functional and structural asymmetry suggest a unifying principle for catalysis in integral membrane-bound pyrophosphatases
J. Strauss, C. Wilkinsion, K. Vidilaseris, O. Ribeiro, J. Liu, J. Hillier, A. Malinen, B. Gehl, L. Jeuken, A. Pearson, A. Goldman
This study presents the first structure of a K+-independent M-PPase and shows asymmetric and time-dependent substrate binding, proposing a unified model for ion pumping and energy coupling in M-PPases.
bioRxiv · Nov 7, 2022Biochemistry