5X5I

The X-ray crystal structure of a TetR family transcription regulator RcdA involved in the regulation of biofilm formation in Escherichia coli

Summary for 5X5I

• Entry DOI: 10.2210/pdb5x5i/pdb
• Descriptor: HTH-type transcriptional regulator RcdA (2 entities in total)
• Functional Keywords: tetr family transcription regulator, master transcription regulator, dimer, biofilm formation, transcription
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 8
• Total formula weight: 176661.50

Authors

Sugino, H.,Usui, M.,Shimada, T.,Nakano, M.,Ogasawara, H.,Ishihama, A.,Hirata, A. (deposition date: 2017-02-16, release date: 2017-12-27, Last modification date: 2024-10-23)

Primary citation

Sugino, H.,Usui, T.,Shimada, T.,Nakano, M.,Ogasawara, H.,Ishihama, A.,Hirata, A.
A structural sketch of RcdA, a transcription factor controlling the master regulator of biofilm formation.
FEBS Lett., 591:2019-2031, 2017

PubMed Abstract: RcdA is a regulator of curlin subunit gene D, the master regulator of biofilm formation in Escherichia coli. Here, we determined the X-ray structure of RcdA at 2.55 Å resolution. RcdA consists of an N-terminal DNA-binding domain (DBD) containing a helix-turn-helix (HTH) motif and a C-terminal dimerization domain, and forms a homodimer in crystals. A computational docking model of the RcdA-DNA complex allowed prediction of the candidate residues responsible for DNA binding. Our structure-guided mutagenesis, in combination with gel shift assay, atomic force microscopic observation, and reporter assay, indicate that R32 in α2 of the HTH motif plays an essential role in the recognition and binding of target DNA while T46 in α3 influences the mode of oligomerization. These results provide insights into the DNA-binding mode of RcdA.

PubMed: 28608551
DOI: 10.1002/1873-3468.12713

Experimental method

X-RAY DIFFRACTION (2.554 Å)