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6P7T

Crystal structure of apo ToxT K231A from Vibrio cholerae strain SCE256

Summary for 6P7T
Entry DOI10.2210/pdb6p7t/pdb
Related6P7R
DescriptorToxin co-regulated pilus virulence regulatory protein (2 entities in total)
Functional Keywordsarac, xyls, virulence regulation, cholerae, dna binding protein
Biological sourceVibrio cholerae
Total number of polymer chains1
Total formula weight32163.10
Authors
Cruite, J.T.,Kull, F.J. (deposition date: 2019-06-06, release date: 2020-01-01, Last modification date: 2024-03-13)
Primary citationCruite, 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: 31815195
DOI: 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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数据于2024-10-30公开中

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