ArticleJournal of biomolecular structure & dynamics2017
Structure and dynamics of the multi-domain resuscitation promoting factor RpfB from Mycobacterium tuberculosis.
Article in Journal of biomolecular structure & dynamics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed.
- Beyond culturability: VBNC-like and differentially culturableFrontiers in cellular and infection microbiology · 2026Review
- Exploring the multifaceted roles of resuscitation-promoting factors in tuberculosis: Implications for diagnosis, vaccine development, and drug targeting.Biotechnology reports (Amsterdam, Netherlands) · 2025Review
- Virulence Factors inBiomolecules · 2023Article
- A Structural View at Vaccine Development againstCells · 2023Review
- Structure-Based Development of SARS-CoV-2 Spike Interactors.International journal of molecular sciences · 2022Article
- Structure based design of effective HtpG-derived vaccine antigens againstFrontiers in molecular biosciences · 2022Article
- Roles of LysM and LytM domains in resuscitation-promoting factor (Rpf) activity and Rpf-mediated peptidoglycan cleavage and dormant spore reactivation.The Journal of biological chemistry · 2020Article
- Resuscitation-Promoting Factors Are Required for Mycobacterium smegmatis Biofilm Formation.Applied and environmental microbiology · 2018Article
- A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Protein science : a publication of the Protein Society · 2018Review
- Collagen-like proteins of pathogenic streptococci.Molecular microbiology · 2017Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
RpfB is multidomain protein that is crucial for Mycobacterium tuberculosis resuscitation from dormancy. This protein cleaves cell wall peptidoglycan, an essential bacterial cell wall polymer formed by glycan chains of β-(1-4)-linked-N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) cross-linked by short peptide stems. RpfB is structurally complex being composed of five distinct domains, namely a catalytic, a G5 and three DUF348 domains. Here, we have undertaken a combined experimental and computation structural investigations on the entire protein to gain insights into its structure-function relationships. CD spectroscopy and light scattering experiments have provided insights into the protein fold stability and into its oligomeric state. Using the available structure information, we modeled the entire protein structure, which includes the two DUF348 domains whose structure is experimentally unknown, and we analyzed the dynamic behavior of RpfB using molecular dynamics simulations. Present results highlight an intricate mutual influence of the dynamics of the different protein domains. These data provide interesting clues on the functional role of non-catalytic domains of RpfB and on the mechanism of peptidoglycan degradation necessary to resuscitation of M. tuberculosis.
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Registered trials
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