Crystal structure of the cofactor‐free form of thioredoxin reductase from <i>Acinetobacter</i> <i>baumannii</i>

Thioredoxin reductase (TrxR) is a central component in the thioredoxin system by involving catalyzing reduction of thioredoxin, which critical for organism survival. Because this essential, it promising target novel antimicrobial agents. Herein, we solved 1.9 Å high‐resolution structure TrxR from Acinetobacter baumannii ( Ab TrxR), Gram‐negative, pathogenic bacterium and drug‐resistant superbug. was cofactor‐free formed dimer solution. contained longer dimerization loop2 shorter β 7 ‐β 8 connecting loop than other TrxRs. form exhibited flavin‐oxidizing (FO) conformation, whose NADPH domain located close to dimeric interface. This structural information might be helpful development new antibiotic agents targeting superbugs.