ArticleThe Journal of biological chemistry2012
Tetrameric structure of the GlfT2 galactofuranosyltransferase reveals a scaffold for the assembly of mycobacterial Arabinogalactan.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 61 citations in OpenAlex.
- Functional (re)annotation ofCurrent research in structural biology · 2025Article
- Substrate binding and catalytic mechanism of UDP-α-D-galactofuranose: β-galactofuranoside β-(1→5)-galactofuranosyltransferase GfsA.PNAS nexus · 2024Article
- Structure, biosynthesis and regulation of the T1 antigen, a phase-variable surface polysaccharide conserved in many Salmonella serovars.Nature communications · 2024Article
- Assessing Squarates as Amine-Reactive Probes.Journal of the American Chemical Society · 2023Article
- An ABC transporter Wzm-Wzt catalyzes translocation of lipid-linked galactan across the plasma membrane in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Progress and challenges in the synthesis of sequence controlled polysaccharides.Beilstein journal of organic chemistry · 2021Review
- Polysaccharide length affects mycobacterial cell shape and antibiotic susceptibility.Science advances · 2020Article
- Catalytic Mechanism of Processive GlfT2: Transition Path Sampling Investigation of Substrate Translocation.ACS omega · 2020Article
- Galactofuranose-Related Enzymes: Challenges and Hopes.International journal of molecular sciences · 2020Review
- A bifunctional O-antigen polymerase structure reveals a new glycosyltransferase family.Nature chemical biology · 2020Article
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Biosynthesis of Galactan inAntibiotics (Basel, Switzerland) · 2020Review
- Synthesis, docking study and biological evaluation of ᴅ-fructofuranosyl and ᴅ-tagatofuranosyl sulfones as potential inhibitors of the mycobacterial galactan synthesis targeting the galactofuranosyltransferase GlfT2.Beilstein journal of organic chemistry · 2020Article
- Article
- Potential Inhibitors of Galactofuranosyltransferase 2 (GlfT2): Molecular Docking, 3D-QSAR, and In Silico ADMETox Studies.Scientific reports · 2019Article
- Essential metabolism for a minimal cell.eLife · 2019Article
- The LPG1x family from Leishmania major is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties.Scientific reports · 2018Article
- Comparing Galactan Biosynthesis inThe Journal of biological chemistry · 2017Article
- Fidelity and Promiscuity of a Mycobacterial Glycosyltransferase.Journal of the American Chemical Society · 2016Article
- Twenty Years of Mycobacterial Glycans: Furanosides and Beyond.Accounts of chemical research · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Biosynthesis of the mycobacterial cell wall relies on the activities of many enzymes, including several glycosyltransferases (GTs). The polymerizing galactofuranosyltransferase GlfT2 (Rv3808c) synthesizes the bulk of the galactan portion of the mycolyl-arabinogalactan complex, which is the largest component of the mycobacterial cell wall. We used x-ray crystallography to determine the 2.45-Å resolution crystal structure of GlfT2, revealing an unprecedented multidomain structure in which an N-terminal β-barrel domain and two primarily α-helical C-terminal domains flank a central GT-A domain. The kidney-shaped protomers assemble into a C(4)-symmetric homotetramer with an open central core and a surface containing exposed hydrophobic and positively charged residues likely involved with membrane binding. The structure of a 3.1-Å resolution complex of GlfT2 with UDP reveals a distinctive mode of nucleotide recognition. In addition, models for the binding of UDP-galactofuranose and acceptor substrates in combination with site-directed mutagenesis and kinetic studies suggest a mechanism that explains the unique ability of GlfT2 to generate alternating β-(1→5) and β-(1→6) glycosidic linkages using a single active site. The topology imposed by docking a tetrameric assembly onto a membrane bilayer also provides novel insights into aspects of processivity and chain length regulation in this and possibly other polymerizing GTs.
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Registered trials
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