4PCV

The structure of BdcA (YjgI) from E. coli

Summary for 4PCV

• Entry DOI: 10.2210/pdb4pcv/pdb
• Descriptor: BdcA (YjgI), TRIETHYLENE GLYCOL, PENTAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: nadp(h) oxidoreductase, oxidoreductase
• Biological source: Escherichia coli P0299438.9
• Total number of polymer chains: 2
• Total formula weight: 50595.72

Authors

Page, R.,Peti, W.,Lord, D. (deposition date: 2014-04-16, release date: 2015-03-11, Last modification date: 2023-12-27)

Primary citation

Lord, D.M.,Baran, A.U.,Wood, T.K.,Peti, W.,Page, R.
BdcA, a protein important for Escherichia coli biofilm dispersal, is a short-chain dehydrogenase/reductase that binds specifically to NADPH.
Plos One, 9:e105751-e105751, 2014

PubMed 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 Å structure 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 Kd of 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.

PubMed: 25244619
DOI: 10.1371/journal.pone.0105751

Experimental method

X-RAY DIFFRACTION (2.05 Å)