6P7T
Crystal structure of apo ToxT K231A from Vibrio cholerae strain SCE256
Summary for 6P7T
Entry DOI | 10.2210/pdb6p7t/pdb |
Related | 6P7R |
Descriptor | Toxin co-regulated pilus virulence regulatory protein (2 entities in total) |
Functional Keywords | arac, xyls, virulence regulation, cholerae, dna binding protein |
Biological source | Vibrio cholerae |
Total number of polymer chains | 1 |
Total formula weight | 32163.10 |
Authors | Cruite, J.T.,Kull, F.J. (deposition date: 2019-06-06, release date: 2020-01-01, Last modification date: 2024-03-13) |
Primary citation | Cruite, J.T.,Kovacikova, G.,Clark, K.A.,Woodbrey, A.K.,Skorupski, K.,Kull, F.J. Structural basis for virulence regulation inVibrio choleraeby unsaturated fatty acid components of bile. Commun Biol, 2:440-440, 2019 Cited by PubMed Abstract: The AraC/XylS-family transcriptional regulator ToxT is the master virulence activator of , the gram-negative bacterial pathogen that causes the diarrheal disease cholera. Unsaturated fatty acids (UFAs) found in bile inhibit the activity of ToxT. Crystal structures of inhibited ToxT bound to UFA or synthetic inhibitors have been reported, but no structure of ToxT in an active conformation had been determined. Here we present the 2.5 Å structure of ToxT without an inhibitor. The structure suggests release of UFA or inhibitor leads to an increase in flexibility, allowing ToxT to adopt an active conformation that is able to dimerize and bind DNA. Small-angle X-ray scattering was used to validate a structural model of an open ToxT dimer bound to the cholera toxin promoter. The results presented here provide a detailed structural mechanism for virulence gene regulation in by the UFA components of bile and other synthetic ToxT inhibitors. PubMed: 31815195DOI: 10.1038/s42003-019-0686-x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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