ArticleScientific reports2016
Structural basis of DNA sequence recognition by the response regulator PhoP in Mycobacterium tuberculosis.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 52 citations in OpenAlex.
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- Serine/threonine protein kinase phosphorylation of DosR alters target gene transcription mechanics and regulates Mycobacterium tuberculosis response to nitric oxide stress.PLoS genetics · 2026Article
- The PhoPQ two-component regulatory system as an important regulator of bacterial stress response.Molecular biology reports · 2025Review
- Structural insights into transcription regulation of the global OmpR/PhoB family regulator PhoP from Mycobacterium tuberculosis.Nature communications · 2025Article
- Structure-guided identification and characterization of potent inhibitors targeting PhoP and MtrA to combat mycobacteria.Computational and structural biotechnology journal · 2024Article
- Molecular mechanism of siderophore regulation by the Pseudomonas aeruginosa BfmRS two-component system in response to osmotic stress.Communications biology · 2024Article
- Analysis of CenKR essentiality in Sinorhizobium meliloti and its activity at a target gene promoter in vivo.FEMS microbiology letters · 2024Article
- Regulatory role ofFrontiers in microbiology · 2024Article
- Pseudomonas aeruginosa two-component system CprRS regulates HigBA expression and bacterial cytotoxicity in response to LL-37 stress.PLoS pathogens · 2024Article
- Structural basis of transcriptional activation by the OmpR/PhoB-family response regulator PmrA.Nucleic acids research · 2023Article
- Substrate DNA Promoting Binding ofMicroorganisms · 2023Article
- Structural basis of phosphorylation-induced activation of the response regulator VbrR.Acta biochimica et biophysica Sinica · 2023Article
- The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.Molecular biomedicine · 2022Review
- Convergence of two global regulators to coordinate expression of essential virulence determinants ofeLife · 2022Article
- Exploring the mono-/bistability range of positively autoregulated signaling systems in the presence of competing transcription factor binding sites.PLoS computational biology · 2022Article
- Genome-Wide Analysis Reveals that PhoP Regulates Pathogenicity in Riemerella anatipestifer.Microbiology spectrum · 2022Article
- Structural insights into DNA binding domain of vancomycin-resistance-associated response regulator in complex with its promoter DNA from Staphylococcus aureus.Protein science : a publication of the Protein Society · 2022Article
- CovS inactivation reduces CovR promoter binding at diverse virulence factor encoding genes in group A Streptococcus.PLoS pathogens · 2022Article
- Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.Acta crystallographica. Section D, Structural biology · 2021Article
- Constitutive expression of the cryptic vanGCd operon promotes vancomycin resistance in Clostridioides difficile clinical isolates.The Journal of antimicrobial chemotherapy · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The transcriptional regulator PhoP is an essential virulence factor in Mycobacterium tuberculosis, and it presents a target for the development of new anti-tuberculosis drugs and attenuated tuberculosis vaccine strains. PhoP binds to DNA as a highly cooperative dimer by recognizing direct repeats of 7-bp motifs with a 4-bp spacer. To elucidate the PhoP-DNA binding mechanism, we determined the crystal structure of the PhoP-DNA complex. The structure revealed a tandem PhoP dimer that bound to the direct repeat. The surprising tandem arrangement of the receiver domains allowed the four domains of the PhoP dimer to form a compact structure, accounting for the strict requirement of a 4-bp spacer and the highly cooperative binding of the dimer. The PhoP-DNA interactions exclusively involved the effector domain. The sequence-recognition helix made contact with the bases of the 7-bp motif in the major groove, and the wing interacted with the adjacent minor groove. The structure provides a starting point for the elucidation of the mechanism by which PhoP regulates the virulence of M. tuberculosis and guides the design of screening platforms for PhoP inhibitors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.