A potential substrate binding pocket of BdcA plays a critical role in NADPH recognition and biofilm dispersal

Biofilm dispersal is characterized by the cell detachment from biofilms and expected to provide novel “anti-biofilm” approaches of prevention and treatment of biofilms in clinical and industrial settings. The E.coli protein BdcA has been identified as a biofilm dispersal factor and designed to be an important component in engineered applications to control biofilm formation. It belongs to short-chain dehydrogenase/reductase (SDR) family with the specific affinity to NADPH. Here, we show the structure of BdcA in complex with NADPH and confirm that NADPH binding is requisite for BdcA facilitating cell motility and increasing biofilm dispersal. Especially, we observe a potential substrate binding pocket surrounded by hydrophobic residues upon NADPH binding and present evidences that this pocket is essential for BdcA binding NADPH and exerting its biological functions. Our study provides the clues for illuminating the molecular mechanism of BdcA regulating biofilm dispersal and better utilizing BdcA to eliminate the biofilms. •The crystal structure of BdcA in complex with NADPH is determined.•NADPH binding stabilizes a potential substrate binding pocket of BdcA.•The substrate binding pocket is conversely involved in BdcA recognizing NADPH.•Both NADPH and substrate binding are essential for BdcA inducing biofilm dispersal.