6KJU

Huge conformation shift of Vibrio cholerae VqmA dimer in the absence of target DNA provides insight into DNA-binding mechanisms of LuxR-type receptors

6KJU の概要

• エントリーDOI: 10.2210/pdb6kju/pdb
• 分子名称: Helix-turn-helix transcriptional regulator, 3,5-dimethylpyrazin-2-ol (3 entities in total)
• 機能のキーワード: vibrio cholera, quorum sensing, transcription regulator, transcription
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57499.88

構造登録者

Wu, H.,Li, M.J.,Guo, H.J.,Zhou, H.,Wang, W.W.,Xu, Q.,Xu, C.Y.,Yu, F.,He, J.H. (登録日: 2019-07-23, 公開日: 2019-11-13, 最終更新日: 2024-10-16)

主引用文献

Wu, H.,Li, M.,Peng, C.,Yin, Y.,Guo, H.,Wang, W.,Xu, Q.,Zhou, H.,Xu, C.,Yu, F.,He, J.
Large conformation shifts of Vibrio cholerae VqmA dimer in the absence of target DNA provide insight into DNA-binding mechanisms of LuxR-type receptors.
Biochem.Biophys.Res.Commun., 520:399-405, 2019

PubMed Abstract: Quorum sensing regulates the biofilm formation and expression of virulence factors in Vibrio cholerae, an obligate human pathogen that continues to imperil human health. Cytoplasmic transcription factor VqmA is a LuxR-type receptor ubiquitous in the Vibrio genus and one vibriophage VP882 and plays an important role in V. cholerae pathogenicity. Here we presented the X-ray crystal structure of V. cholerae VqmA-DPO complex and compared it with the previously determined VqmA-DPO-DNA complex. To our knowledge, this is the first report on the crystal structures of the same LuxR-type receptor with two conformations of binding to DNA and not binding to DNA. Based on the results of structural analysis and biochemical assays, we revealed the secondary structure of the linker region between two function domains changed significantly, and DNA binding domains were covalently linked by a disulfide bond formed by the highly conserved Cys134. Besides, the distance between two DBD monomers became longer than that in DNA-binding conformation, and two α8 helixes underwent a large conformation shift. The results of the structure-function analyses presented here improve our understanding of the complex mechanisms in the conformational changes of LuxR-type receptors caused by DNA binding.

PubMed: 31606206
DOI: 10.1016/j.bbrc.2019.10.063

実験手法

X-RAY DIFFRACTION (1.75 Å)