5z2l
Crystal structure of BdcA in complex with NADPH
Structural highlights
FunctionBDCA_ECOLI Increases biofilm dispersal. Acts by binding directly to the signaling molecule cyclic-di-GMP, which decreases the intracellular concentration of cyclic-di-GMP and leads to biofilm dispersal. Also controls other biofilm-related phenotypes such as cell motility, cell size, cell aggregation and production of extracellular DNA and extracellular polysaccharides (EPS). Does not act as a phosphodiesterase.[1] Publication Abstract from PubMedBiofilm 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. A potential substrate binding pocket of BdcA plays a critical role in NADPH recognition and biofilm dispersal.,Yang WS, Hong Y, Zhang Y, Wang DC, Li DF, Hou YJ Biochem Biophys Res Commun. 2018 Mar 11;497(3):863-868. doi:, 10.1016/j.bbrc.2018.02.143. Epub 2018 Feb 17. PMID:29462616[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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