BdcA, a protein important for escherichia coli biofilm dispersal, is a short-chain dehydrogenase/reductase that binds specifically to NADPH

Dana M. Lord, Ayse Uzgoren Baran, Thomas K. Wood, Wolfgang Peti, Rebecca Page

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The Escherichia coli protein BdcA (previously referred to as YjgI) plays a key role in the dispersal of cells from bacterial biofilms, and its constitutive activation provides an attractive therapeutic target for dismantling these communities. In order to investigate the function of BdcA at a molecular level, we integrated structural and functional studies. Our 2.05 Astructure of BdcA shows that it is a member of the NAD(P)(H)-dependent short-chain dehydrogenase/reductase (SDR) superfamily. Structural comparisons with other members of the SDR family suggested that BdcA binds NADP(H). This was demonstrated experimentally using thermal denaturation studies, which showed that BcdA binds specifically to NADPH. Subsequent ITC experiments further confirmed this result and reported a Kdof 25.9 μM. Thus, BdcA represents the newest member of the limited number of oxidoreductases shown to be involved in quorum sensing and biofilm dispersal.

Original languageEnglish (US)
Article numbere105751
JournalPloS one
Volume9
Issue number9
DOIs
StatePublished - Sep 22 2014

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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