ArticleOpen biology2016
Structural and functional analysis of the solute-binding protein UspC from Mycobacterium tuberculosis that is specific for amino sugars.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Metabolic flexibility and an unusual route for peptidoglycan muramic acid recycling in mycobacteria.The Journal of biological chemistry · 2026Article
- Interrogation of the Pathogen Box reveals small molecule ligands against the mycobacterial trehalose transporter LpqY-SugABC.RSC medicinal chemistry · 2022Article
- Biochemical and phenotypic characterisation of theCell surface (Amsterdam, Netherlands) · 2021Article
- Comparison of carbohydrate ABC importers from Mycobacterium tuberculosis.BMC genomics · 2021Article
- Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope.Chemical reviews · 2021Review
- Synthesis and recycling of the mycobacterial cell envelope.Current opinion in microbiology · 2021Review
- Physicochemical properties andRSC medicinal chemistry · 2020Review
- The ATP-Binding Cassette (ABC) Transport Systems inBiology · 2020Review
- ATP-binding cassette (ABC) import systems ofEmerging microbes & infections · 2020Review
- Structural Basis of Glycerophosphodiester Recognition by theACS chemical biology · 2019Article
- The prominent alteration in transcriptome and metabolome of Mycobacterium bovis BCG str. Tokyo 172 induced by vitamin BBMC microbiology · 2019Article
- Structural and functional determination of homologs of theThe Journal of biological chemistry · 2018Article
- Modeling the Metabolic State ofFrontiers in cellular and infection microbiology · 2018Article
- Genome scale identification, structural analysis, and classification of periplasmic binding proteins from Mycobacterium tuberculosis.Current genetics · 2017Article
- Structural basis of trehalose recognition by the mycobacterial LpqY-SugABC transporter.The Journal of biological chemistryArticle
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Mycobacterium tuberculosis (Mtb), the aetiological agent of tuberculosis, has evolved to scavenge nutrients from the confined environment of host macrophages with mycobacterial ATP-binding cassette (ABC) transporters playing a key role in nutrient acquisition. Mtb-UspC (Rv2318) is the solute-binding protein of the essential transporter UspABC, one of four Mtb ABC transporters implicated by homology in sugar acquisition. Herein, we report the structural and functional characterization of Mtb-UspC. The 1.5 Å resolution structure of UspC reveals a two subdomain architecture that forms a highly acidic carbohydrate-substrate binding cleft. This has allowed a distinct preference of Mtb-UspC for amino sugars as determined by thermal shift analysis and solution saturation transfer difference-NMR. Taken together our data support the functional assignment of UspABC as an amino-sugar transporter. Given the limited availability of carbohydrates within the phagosomal environmental niche during Mtb intracellular infection, our studies suggest that UspABC enables Mtb to optimize the use of scarce nutrients during intracellular infection, linking essentiality of this protein to a potential role in recycling components of cell-wall peptidoglycan.
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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.