Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation
N. Noby, H. Sabah Auhim, H. Worthy, S. Winter, A. Embady, H. Saeed, A. Hussein, C. Pudney, P. Rizkallah, S. A. Wells, D. Jones, C. R. Pudney
This study determines the structure of a cold-active esterase and identifies increased substrate accessibility and water entropy tolerance as the main drivers of its cold adaptation.
bioRxiv · Feb 23, 2021 · PreprintBiochemistry