Extended Data Fig. 7: NicA2 wildtype and v321 have similar structures when bound by N-methylmyosmine.

We first attempted to crystallize NicA2 v320, but none of our crystals diffracted to adequate resolution for structure determination. We were fortunate to obtain well diffracting crystals of NicA2 v321 in both the ligand-free and NMM-bound forms. The mutational changes and kinetic parameters of v320 and v321 are similar, so the structural perturbations seen for v321 are likely informative for those in v320 and other variants that contain similar changes. a, Unbound NicA2 wildtype (PDB: 5TTJ) and v321 enzyme structures were overlaid, aligned at their flavin binding domains. b, Overlay of the active sites of the enzymes with A107T and H368R mutations rendered. c, NicA2 wildtype and v321 enzyme structures bound to N-methylmyosmine were overlaid, aligned at their flavin binding domains. d, Overlay of the active sites with A107T and H368R mutations rendered. Wildtype enzyme is rendered in cyan/blue, v321 in orange/salmon, Flavin adenine dinucleotide in yellow, and N-methylmyosmine in magenta.