5Z2L

Crystal structure of BdcA in complex with NADPH

5Z2L の概要

• エントリーDOI: 10.2210/pdb5z2l/pdb
• 分子名称: Cyclic-di-GMP-binding biofilm dispersal mediator protein, 2-(2-METHOXYETHOXY)ETHANOL, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (8 entities in total)
• 機能のキーワード: short-chain dehydrogenase/reductase (sdr), nadph binding, biofilm dispersal, oxidoreductase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 318289.51

構造登録者

Yang, W.S.,Hou, Y.J.,Li, D.F.,Wang, D.C. (登録日: 2018-01-03, 公開日: 2018-03-07, 最終更新日: 2023-11-22)

主引用文献

Yang, W.S.,Hong, Y.,Zhang, Y.,Wang, D.C.,Li, D.F.,Hou, Y.J.
A potential substrate binding pocket of BdcA plays a critical role in NADPH recognition and biofilm dispersal
Biochem. Biophys. Res. Commun., 497:863-868, 2018

PubMed 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.

PubMed: 29462616
DOI: 10.1016/j.bbrc.2018.02.143

実験手法

X-RAY DIFFRACTION (1.7 Å)