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To understand the catalytic mechanism of the ADP-ribosylhydrolase (ARH) activity of MavL, we screened its active truncation mutants and succeeded in solving the structure of the MavL 40-404 -ADPR complex at a resolution of 2.38 , which revealed that several pairs of hydrogen bonds and a - stacking interaction provided by surrounding amino acids or water molecules are involved in interactions between MavL and ADPR (Supplementary Fig

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Analysis of root-mean-square deviation (RMSD) of GLRX over the course of MD simulations before and after each mutation confirmed that the overall fold of GLRX was not altered by these mutations (Supplementary Fig

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