ArticleBiochemistry2007
Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- 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
- Article
- Residue coevolution and mutational landscape for OmpR and NarL response regulator subfamilies.Biophysical journal · 2024Article
- Structural basis of DNA recognition of themBio · 2024Article
- Structural insights into the transcription activation mechanism of the global regulator GlnR from actinobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural basis of phosphorylation-induced activation of the response regulator VbrR.Acta biochimica et biophysica Sinica · 2023Article
- The Bacterial MtrAB Two-Component System Regulates the Cell Wall Homeostasis Responding to Environmental Alkaline Stress.Microbiology spectrum · 2022Article
- Two-component sensor histidine kinases of Mycobacterium tuberculosis: Beacons for niche navigation.Molecular microbiology · 2022Review
- Mutation of MtrA at the Predicted Phosphorylation Site Abrogates Its Role as a Global Regulator in Streptomyces venezuelae.Microbiology spectrum · 2022Article
- Regulation of Resistance in Vancomycin-Resistant Enterococci: The VanRS Two-Component System.Microorganisms · 2021Review
- Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.Acta crystallographica. Section D, Structural biology · 2021Article
- Methylation of two-component response regulator MtrA in mycobacteria negatively modulates its DNA binding and transcriptional activation.The Biochemical journal · 2020Article
- Epistatic Effect of Regulators to the Adaptive Growth of Escherichia coli.Scientific reports · 2020Article
- DNA-Binding and Transcription Activation by Unphosphorylated Response Regulator AgrR FromFrontiers in microbiology · 2020Article
- RitR is an archetype for a novel family of redox sensors in the streptococci that has evolved from two-component response regulators and is required for pneumococcal colonization.PLoS pathogens · 2018Article
- Multisystem Analysis ofmBio · 2018Article
- MtrA Response Regulator Controls Cell Division and Cell Wall Metabolism and Affects Susceptibility of Mycobacteria to the First Line Antituberculosis Drugs.Frontiers in microbiology · 2018Article
- To ∼P or Not to ∼P? Non-canonical activation by two-component response regulators.Molecular microbiology · 2017Review
- The Conserved Actinobacterial Two-Component System MtrAB Coordinates Chloramphenicol Production with Sporulation inFrontiers in microbiology · 2017Article
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7 authors.
Funding
Abstract
The structure of MtrA, an essential gene product for the human pathogen Mycobacterium tuberculosis, has been solved to a resolution of 2.1 A. MtrA is a member of the OmpR/PhoB family of response regulators and represents the fourth family member for which a structure of the protein in its inactive state has been determined. As is true for all OmpR/PhoB family members, MtrA possesses an N-terminal regulatory domain and a C-terminal winged helix-turn-helix DNA-binding domain, with phosphorylation of the regulatory domain modulating the activity of the protein. In the inactive form of MtrA, these two domains form an extensive interface that is composed of the alpha4-beta5-alpha5 face of the regulatory domain and the C-terminal end of the positioning helix, the trans-activation loop, and the recognition helix of the DNA-binding domain. This domain orientation suggests a mechanism of mutual inhibition by the two domains. Activation of MtrA would require a disruption of this interface to allow the alpha4-beta5-alpha5 face of the regulatory domain to form the intermolecule interactions that are associated with the active state and to allow the recognition helix to interact with DNA. Furthermore, the interface appears to stabilize the inactive conformation of MtrA, potentially reducing the rate of phosphorylation of the N-terminal domain. This combination of effects may form a switch, regulating the activity of MtrA. The domain orientation exhibited by MtrA also provides a rationale for the variation in linker length that is observed within the OmpR/PhoB family of response regulators.
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