ArticleActa crystallographica. Section D, Biological crystallography2013
Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- A color-tailored fluorogenic sensor for hydrogen peroxide.Nature chemical biology · 2026Article
- Generalization of Young-Laplace, Kelvin, and Gibbs-Thomson equations for arbitrarily curved surfaces.Biophysical journal · 2023Article
- How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes.Antioxidants (Basel, Switzerland) · 2021Review
- Insertional Inactivation ofMicroorganisms · 2021Article
- Structural snapshots of OxyR reveal the peroxidatic mechanism of HProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Tolerance to oxidative stress is required for maximal xylem colonization by the xylem-limited bacterial phytopathogen, Xylella fastidiosa.Molecular plant pathology · 2017Article
- The hydrogen peroxide hypersensitivity of OxyR2 inThe Journal of biological chemistry · 2017Article
- Structural details of the OxyR peroxide-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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5 authors at 1 institution in 1 country.
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Abstract
OxyR transcriptionally regulates Escherichia coli oxidative stress response genes through a reversibly reducible cysteine disulfide biosensor of cellular redox status. Structural changes induced by redox changes in these cysteines are conformationally transmitted to the dimer subunit interfaces, which alters dimer and tetramer interactions with DNA. In contrast to E. coli OxyR regulatory-domain structures, crystal structures of Porphyromonas gingivalis OxyR regulatory domains show minimal differences in dimer configuration on changes in cysteine disulfide redox status. This locked configuration of the P. gingivalis OxyR regulatory-domain dimer closely resembles the oxidized (activating) form of the E. coli OxyR regulatory-domain dimer. It correlates with the observed constitutive activation of some oxidative stress genes in P. gingivalis and is attributable to a single amino-acid insertion in P. gingivalis OxyR relative to E. coli OxyR. Modelling of full-length P. gingivalis, E. coli and Neisseria meningitidis OxyR-DNA complexes predicts different modes of DNA binding for the reduced and oxidized forms of each.
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