A potential substrate binding pocket of BdcA plays a critical role in NADPH recognition and biofilm dispersal.
Biochem Biophys Res Commun
; 497(3): 863-868, 2018 03 11.
Article
en En
| MEDLINE
| ID: mdl-29462616
ABSTRACT
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.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Biopelículas
/
Proteínas de Escherichia coli
/
Escherichia coli
/
NADP
Tipo de estudio:
Prognostic_studies
Idioma:
En
Año:
2018
Tipo del documento:
Article