ArticleNucleic acids research2024
Structural basis of transcriptional regulation by UrtR in response to uric acid.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- β-Propeller structure of the CJ1041C protein from Campylobacter jejuni and its interaction with CaScientific reports · 2026Article
- A DNA damage-activated kinase phosphorylates a transcriptional repressor to control bacterial immune pathway expression.The EMBO journal · 2026Article
- Article
- A DNA damage-activated kinase controls bacterial immune pathway expression.bioRxiv : the preprint server for biology · 2026Article
- Structural Analysis of the Putative Succinyl-Diaminopimelic Acid Desuccinylase DapE fromCurrent issues in molecular biology · 2025Article
- Crystal structures of Campylobacter jejuni CadF reveal a potential role for the arginine residue R268 in peptidoglycan recognition and pocket formation.Scientific reports · 2025Article
- Structural analysis of YcdY, a member of the redox-enzyme maturation protein family.Acta crystallographica. Section F, Structural biology communications · 2025Article
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6 authors.
Funding
Abstract
Uric acid (UA)-responsive transcriptional regulators (UrtRs), which belong to the multiple antibiotic resistance regulator (MarR) superfamily, transcriptionally coordinate virulence and metabolism in bacteria by modulating interactions with operator DNA in response to UA. To elucidate the transcriptional regulatory mechanism of UrtR, we structurally analyzed UrtR proteins, including PecS, MftR, and HucR, alone and in complex with UA or DNA. UrtR contains a dimerization domain (DD) and a winged helix-turn-helix domain (wHTHD) and forms a homodimer primarily via the DD, as observed for other MarR superfamily proteins. However, UrtRs are characterized by a unique N-terminal α-helix, which contributes to dimerization and UA recognition. In the absence of UA, the UrtR dimer symmetrically binds to the operator double-stranded DNA (dsDNA) by inserting its α4 recognition helix and β-stranded wing within the wHTHD into the major and minor grooves of dsDNA, respectively. Upon exposure to UA, UrtR accommodates UA in the intersubunit pocket between the DD and wHTHD. UA binding induces a conformational change in the major groove-binding core element of the UrtR wHTHD, generating a DNA binding-incompatible structure. This local allosteric mechanism of UrtR completely differs from that generally observed in other MarR superfamily members, in which the entire wHTHD undergoes effector-responsive global shifts.
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