6UTC

Intra-chain disulfide bonded ToxR periplasmic domain from Vibrio vulnificus

Summary for 6UTC

• Entry DOI: 10.2210/pdb6utc/pdb
• Descriptor: Transcriptional activator ToxR, SULFATE ION (3 entities in total)
• Functional Keywords: sensor, periplasm, toxr, alpha-beta, dna binding protein
• Biological source: Vibrio vulnificus
• Total number of polymer chains: 1
• Total formula weight: 11745.17

Authors

Midgett, C.R.,Swindell, R.A.,Kull, F.J. (deposition date: 2019-10-29, release date: 2020-06-17, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.249 Å)