ArticleActa crystallographica. Section D, Structural biology2019
Nitrosative stress sensing in Porphyromonas gingivalis: structure of and heme binding by the transcriptional regulator HcpR.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- A nitrite-responsive regulatory RNA locus sustains commensal resilience against nitrosative stress.bioRxiv : the preprint server for biology · 2026Article
- Article
- cAMP-independent Crp homolog adds to the multi-layer regulatory network inFrontiers in cellular and infection microbiology · 2025Article
- Sequence and characterization of shuttle vectors for molecular cloning in Porphyromonas, Bacteroides and related bacteria.Molecular oral microbiology · 2020Article
- Article
- PgRsp Is a Novel Redox-Sensing Transcription Regulator Essential forMicroorganisms · 2019Article
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6 authors.
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Abstract
Although the HcpR regulator plays a vital step in initiation of the nitrosative stress response in many Gram-negative anaerobic bacteria, the molecular mechanisms that it uses to mediate gas sensing are not well understood. Here, a 2.6 Å resolution crystal structure of the N-terminal sensing domain of the anaerobic periodontopathogen Porphyromonas gingivalis HcpR is presented. The protein has classical features of the regulators belonging to the FNR-CRP family and contains a hydrophobic pocket in its N-terminal sensing domain. It is shown that heme bound to HcpR exhibits heme iron as a hexacoordinate system in the absence of nitric oxide (NO) and that upon nitrosylation it transitions to a pentacoordinate system. Finally, small-angle X-ray scattering experiments on full-length HcpR reveal that the C-terminal DNA-binding domain of HcpR has a high degree of interdomain flexibility.
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