ArticleNature communications2025
Structural insights into terminal arabinosylation of mycobacterial cell wall arabinan.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Super-Armed Thiomannopyranosides in the Synthesis of a Mannose-Capped Trisaccharide ofMolecules (Basel, Switzerland) · 2026Article
- A periplasmic protein complex mediates arabinofuranosyltransferase activity and intrinsic drug resistance inScience advances · 2026Article
- A new role for lipoproteins LpqZ and FecB in orchestrating mycobacterial cell envelope biogenesis.mBio · 2026Article
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Expression and Purification of Integral Membrane Enzymes for Functional and Structural Studies.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Breaking the barrier: from biosynthetic inhibition to multidimensional modulation of the mycobacterial cell wall in tuberculosis therapy.Frontiers in pharmacology · 2026Review
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
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20 authors.
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Abstract
The global challenge of tuberculosis, caused by Mycobacterium tuberculosis (Mtb), is compounded by the emergence of drug-resistant strains. A critical factor in Mtb's pathogenicity is its intricate cell envelope, which acts as a formidable barrier against immune defences and pharmacological interventions. Central to this envelope are arabinogalactan (AG) and lipoarabinomannan (LAM), two complex polysaccharides containing arabinan domains essential for maintaining cell wall structure and function. The arabinofuranosyltransferase AftB plays a pivotal role in the biosynthesis of these arabinan domains by catalyzing the addition of β-(1 → 2)-linked terminal arabinofuranose residues. Here, we present the cryo-EM structures of Mycobacterium chubuense AftB in both its apo form and bound to a donor substrate analog, resolved at 2.9 Å and 3.4 Å resolution, respectively. These structures reveal that AftB has a GT-C fold, with a transmembrane (TM) domain comprised of eleven TM helices and a periplasmic cap domain. AftB has a distinctive irregular, tube-shaped cavity that connects two proposed substrate binding sites. Through an integrated approach combining structural analysis, biochemical assays, and molecular dynamics simulations, we delineate the molecular basis of AftB's reaction mechanism and propose a model for its catalytic function.
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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.