ArticleActa crystallographica. Section D, Structural biology2021
Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.
Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Residue coevolution and mutational landscape for OmpR and NarL response regulator subfamilies.Biophysical journal · 2024Article
- Trends in the two-component system's role in the synthesis of antibiotics by Streptomyces.Applied microbiology and biotechnology · 2023Review
- Progress in the Prevalence, Classification and Drug Resistance Mechanisms of Methicillin-ResistantInfection and drug resistance · 2023Review
- Two-Component Systems ofInternational journal of molecular sciences · 2022Review
- Dysgonomonas mossii Strain Shenzhen WH 0221, a New Member of the GenusMicrobiology spectrum · 2022Article
- Analytical Ultracentrifugation as a Matrix-Free Probe for the Study of Kinase Related Cellular and Bacterial Membrane Proteins and Glycans.Molecules (Basel, Switzerland) · 2021Review
- Regulation of Resistance in Vancomycin-Resistant Enterococci: The VanRS Two-Component System.Microorganisms · 2021Review
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Authors and funding
5 authors.
Funding
Abstract
Vancomycin has historically been used as a last-resort treatment for serious bacterial infections. However, vancomycin resistance has become widespread in certain pathogens, presenting a serious threat to public health. Resistance to vancomycin is conferred by a suite of resistance genes, the expression of which is controlled by the VanR-VanS two-component system. VanR is the response regulator in this system; in the presence of vancomycin, VanR accepts a phosphoryl group from VanS, thereby activating VanR as a transcription factor and inducing expression of the resistance genes. This paper presents the X-ray crystal structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states at resolutions of 2.3 and 2.0 Å, respectively. Comparison of the two structures illustrates that phosphorylation of VanR is accompanied by a disorder-to-order transition of helix 4, which lies within the receiver domain of the protein. This transition generates an interface that promotes dimerization of the receiver domain; dimerization in solution was verified using analytical ultracentrifugation. The inactive conformation of the protein does not appear intrinsically unable to bind DNA; rather, it is proposed that in the activated form DNA binding is enhanced by an avidity effect contributed by the receiver-domain dimerization.
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