6UTC

Intra-chain disulfide bonded ToxR periplasmic domain from Vibrio vulnificus

6UTC の概要

• エントリーDOI: 10.2210/pdb6utc/pdb
• 分子名称: Transcriptional activator ToxR, SULFATE ION (3 entities in total)
• 機能のキーワード: sensor, periplasm, toxr, alpha-beta, dna binding protein
• 由来する生物種: Vibrio vulnificus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11745.17

構造登録者

Midgett, C.R.,Swindell, R.A.,Kull, F.J. (登録日: 2019-10-29, 公開日: 2020-06-17, 最終更新日: 2024-11-13)

主引用文献

Midgett, C.R.,Swindell, R.A.,Pellegrini, M.,Jon Kull, F.
A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts.
Sci Rep, 10:9002-9002, 2020

PubMed Abstract: ToxR is a transmembrane transcription factor that, together with its integral membrane periplasmic binding partner ToxS, is conserved across the Vibrionaceae family. In some pathogenic Vibrios, including V. parahaemolyticus and V. cholerae, ToxR is required for bile resistance and virulence, and ToxR is fully activated and protected from degradation by ToxS. ToxS achieves this in part by ensuring formation of an intra-chain disulfide bond in the C-terminal periplasmic domain of ToxR (dbToxRp). In this study, biochemical analysis showed dbToxRp to have a higher affinity for the ToxS periplasmic domain than the non-disulfide bonded conformation. Analysis of our dbToxRp crystal structure showed this is due to disulfide bond stabilization. Furthermore, dbToxRp is structurally homologous to the V. parahaemolyticus VtrA periplasmic domain. These results highlight the critical structural role of disulfide bond in ToxR and along with VtrA define a domain fold involved in environmental sensing conserved across the Vibrionaceae family.

PubMed: 32488093
DOI: 10.1038/s41598-020-66050-5

実験手法

X-RAY DIFFRACTION (1.249 Å)