ArticleBiophysical journal2013
Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Exploring the multifaceted roles of resuscitation-promoting factors in tuberculosis: Implications for diagnosis, vaccine development, and drug targeting.Biotechnology reports (Amsterdam, Netherlands) · 2025Review
- Anti-tubercular activity evaluation of natural compounds by targeting Mycobacterium tuberculosis resuscitation promoting factor B inhibition: An in silico study.Molecular diversity · 2024Article
- Article
- Unveiling CD59-Antibody Interactions to Design Paratope-Mimicking Peptides for Complement Modulation.International journal of molecular sciences · 2023Article
- Computer-aided identification ofFrontiers in pharmacology · 2023Article
- Article
- Structure-Based Development of SARS-CoV-2 Spike Interactors.International journal of molecular sciences · 2022Article
- On the Identification of Clinically Relevant Bacterial Amino Acid Changes at the Whole Genome Level Using Auto-PSS-Genome.Interdisciplinary sciences, computational life sciences · 2021Article
- PE_PGRS33, an Important Virulence Factor ofCells · 2021Review
- Identification andHeliyon · 2020Article
- Desolvation of the substrate-binding protein TauA dictates ligand specificity for the alkanesulfonate ABC importer TauABC.The Biochemical journal · 2019Article
- The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial Cytokinesis: A Structural Perspective.Cells · 2019Review
- Resuscitation-Promoting Factors Are Required for Mycobacterium smegmatis Biofilm Formation.Applied and environmental microbiology · 2018Article
- Characterising resuscitation promoting factor fluorescent-fusions in mycobacteria.BMC microbiology · 2018Article
- A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Protein science : a publication of the Protein Society · 2018Review
- Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017Review
- Structure and dynamics of the multi-domain resuscitation promoting factor RpfB from Mycobacterium tuberculosis.Journal of biomolecular structure & dynamics · 2017Article
- Substrate recognition and catalysis by LytB, a pneumococcal peptidoglycan hydrolase involved in virulence.Scientific reports · 2015Article
- Mycobacterial Growth.Cold Spring Harbor perspectives in medicine · 2015Review
- NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain.PloS one · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resuscitation of Mtb is crucial to the etiology of Tuberculosis, because latent tuberculosis is estimated to affect one-third of the world population. The resuscitation-promoting factor RpfB is mainly responsible for Mtb resuscitation from dormancy. Given the impact of latent Tuberculosis, RpfB represents an interesting target for tuberculosis drug discovery. However, no molecular models of substrate binding and catalysis are hitherto available for this enzyme. Here, we identified key interactions involved in substrate binding to RpfB by combining x-ray diffraction studies and computational approaches. The crystal structure of RpfB catalytic domain in complex with N,N',N"-triacetyl-chitotriose, as described here, provides the first, to our knowledge, atomic representation of ligand recognition by RpfB and demonstrates that the strongest interactions are established by the N-acetylglucosamine moiety in the central region of the enzyme binding cleft. Molecular dynamics analyses provided information on the dynamic behavior of protein-substrate interactions and on the role played by the solvent in RpfB function. These data combined with sequence conservation analysis suggest that Glu-292 is the sole residue crucial for catalysis, implying that RpfB acts via the formation of an oxocarbenium ion rather than a covalent intermediate. Present data represent a solid base for the design of effective drug inhibitors of RpfB. Moreover, homology models were generated for the catalytic domains of all members of the Mtb Rpf family (RpfA-E). The analysis of these models unveiled analogies and differences among the different members of the Rpf protein family.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.