ArticleBiochemistry2011
Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domain.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Transcriptional control of asparagine utilization regulates mycobacterial pH-driven adaptation at the host-pathogen crossroads.The Journal of biological chemistry · 2026Article
- The PhoPQ two-component regulatory system as an important regulator of bacterial stress response.Molecular biology reports · 2025Review
- ENcyclopedia of TRAnscription Factors in Bacteria and Archaea genomes (ENTRAF) version 2.0.Database : the journal of biological databases and curation · 2025Article
- Exploring virulence in Mycobacterium bovis: clues from comparative genomics and perspectives for the future.Irish veterinary journal · 2023Review
- 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
- Structure of the Acinetobacter baumannii PmrA receiver domain and insights into clinical mutants affecting DNA binding and promoting colistin resistance.Journal of biochemistry · 2022Article
- Identification of drivers of mycobacterial resistance to peptidoglycan synthesis inhibitors.Frontiers in microbiology · 2022Article
- Bacterial two-component systems as sensors for synthetic biology applications.Current opinion in systems biology · 2021Article
- Methylation of PhoP by CheR RegulatesmBio · 2021Article
- Acetylation of PhoP K88 Is Involved in RegulatingInfection and immunity · 2021Article
- Regulation of gene expression by protein lysine acetylation in Salmonella.Journal of microbiology (Seoul, Korea) · 2020Review
- Identification of Uncharacterized Components of Prokaryotic Immune Systems and Their Diverse Eukaryotic Reformulations.Journal of bacteriology · 2020Article
- Epistatic Effect of Regulators to the Adaptive Growth of Escherichia coli.Scientific reports · 2020Article
- Article
- Rewiring bacterial two-component systems by modular DNA-binding domain swapping.Nature chemical biology · 2019Article
- Metabolic intermediate acetyl phosphate modulates bacterial virulence via acetylation.Emerging microbes & infections · 2019Article
- Role of CovR phosphorylation in gene transcription in Streptococcus mutans.Microbiology (Reading, England) · 2018Article
- Inhibition of the DevSR Two-Component System by Overexpression of Mycobacterium tuberculosis PknB in Mycobacterium smegmatis.Molecules and cells · 2017Article
- Asymmetric Structure of the Dimerization Domain of PhoR, a Sensor Kinase Important for the Virulence ofACS omega · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
Abstract
The PhoP protein from Mycobacterium tuberculosis is a response regulator of the OmpR/PhoB subfamily, whose structure consists of an N-terminal receiver domain and a C-terminal DNA-binding domain. How the DNA-binding activities are regulated by phosphorylation of the receiver domain remains unclear due to a lack of structural information on the full-length proteins. Here we report the crystal structure of the full-length PhoP of M. tuberculosis. Unlike other known structures of full-length proteins of the same subfamily, PhoP forms a dimer through its receiver domain with the dimer interface involving α4-β5-α5, a common interface for activated receiver domain dimers. However, the switch residues, Thr99 and Tyr118, are in a conformation resembling those of nonactivated receiver domains. The Tyr118 side chain is involved in the dimer interface interactions. The receiver domain is tethered to the DNA-binding domain through a flexible linker and does not impose structural constraints on the DNA-binding domain. This structure suggests that phosphorylation likely facilitates/stabilizes receiver domain dimerization, bringing the DNA-binding domains to close proximity, thereby increasing their binding affinity for direct repeat DNA sequences.
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