6P7T

Crystal structure of apo ToxT K231A from Vibrio cholerae strain SCE256

6P7T の概要

• エントリーDOI: 10.2210/pdb6p7t/pdb
• 関連するPDBエントリー: 6P7R
• 分子名称: Toxin co-regulated pilus virulence regulatory protein (2 entities in total)
• 機能のキーワード: arac, xyls, virulence regulation, cholerae, dna binding protein
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32163.10

構造登録者

Cruite, J.T.,Kull, F.J. (登録日: 2019-06-06, 公開日: 2020-01-01, 最終更新日: 2024-03-13)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.5 Å)