PDBsum entry 6utc

DNA binding protein

PDB id: 6utc

Contents

Protein chain

91 a.a.

Ligands

SO4

Waters ×104

PDB id:

6utc

Name:

DNA binding protein

Title:

Intra-chain disulfide bonded toxr periplasmic domain from vibrio vulnificus

Structure:

Transcriptional activator toxr. Chain: a. Fragment: periplasmic domain. Synonym: transcriptional regulator,transmembrane transcription activator. Engineered: yes

Source:

Vibrio vulnificus. Organism_taxid: 672. Gene: toxr, crn46_04050, d8t65_08455, forc36_0761. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.25Å R-factor: 0.194 R-free: 0.213

Authors:

C.R.Midgett,R.A.Swindell,F.J.Kull

Key ref:

C.R.Midgett et al. (2020). A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts. Sci Rep, 10, 9002. PubMed id: 32488093 DOI: 10.1038/s41598-020-66050-5

Date:

29-Oct-19 Release date: 17-Jun-20

Protein chain

Q9RP86  (Q9RP86_VIBVL) -  Transcriptional regulator from Vibrio vulnificus

Seq: 290 a.a.

Struc: 91 a.a.

DOI no: 10.1038/s41598-020-66050-5

Sci Rep 10:9002 (2020)

PubMed id: 32488093

A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts.

C.R.Midgett, R.A.Swindell, M.Pellegrini, F.Jon Kull.

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.