ArticleProtein science : a publication of the Protein Society2014
Three-dimensional structure of a sugar N-formyltransferase from Francisella tularensis.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 21 citations in OpenAlex.
- Mutation ofMicrobiology (Reading, England) · 2024Article
- Structure and function of an N-acetyltransferase from the human pathogen Acinetobacter baumannii isolate BAL_212.Proteins · 2022Article
- Why vary what's working? Phase variation and biofilm formation inFrontiers in microbiology · 2022Review
- Investigation of the enzymes required for the biosynthesis of an unusual formylated sugar in the emerging human pathogen Helicobacter canadensis.Protein science : a publication of the Protein Society · 2021Article
- Biochemical analysis of a sugar 4,6-dehydratase from Acanthamoeba polyphaga Mimivirus.Protein science : a publication of the Protein Society · 2020Article
- Misannotations of the genes encoding sugar N-formyltransferases.Protein science : a publication of the Protein Society · 2020Article
- Investigation of a sugar N-formyltransferase from the plant pathogen Pantoea ananatis.Protein science : a publication of the Protein Society · 2019Article
- PvdF of pyoverdin biosynthesis is a structurally unique NArchives of biochemistry and biophysics · 2019Article
- The Mycobacterium tuberculosis complex has a pathway for the biosynthesis of 4-formamido-4,6-dideoxy-d-glucose.Protein science : a publication of the Protein Society · 2018Article
- Molecular architecture of an N-formyltransferase from Salmonella enterica O60.Journal of structural biology · 2017Article
- Biochemical Investigation of Rv3404c from Mycobacterium tuberculosis.Biochemistry · 2017Article
- Biochemical Characterization of WbkC, an N-Formyltransferase from Brucella melitensis.Biochemistry · 2017Article
- Enzymes required for the biosynthesis of N-formylated sugars.Current opinion in structural biology · 2016Review
- Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N.Protein science : a publication of the Protein Society · 2016Article
- Bacterial Sugar 3,4-Ketoisomerases: Structural Insight into Product Stereochemistry.Biochemistry · 2015Article
- Molecular structure of an N-formyltransferase from Providencia alcalifaciens O30.Protein science : a publication of the Protein Society · 2015Article
- New role for the ankyrin repeat revealed by a study of the N-formyltransferase from Providencia alcalifaciens.Biochemistry · 2015Article
- Comparative review of Francisella tularensis and Francisella novicida.Frontiers in cellular and infection microbiology · 2014Review
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3 authors at 1 institution in 1 country.
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Abstract
N-formylated sugars have been observed on the O-antigens of such pathogenic Gram-negative bacteria as Campylobacter jejuni and Francisella tularensis. Until recently, however, little was known regarding the overall molecular architectures of the N-formyltransferases that are required for the biosynthesis of these unusual sugars. Here we demonstrate that the protein encoded by the wbtj gene from F. tularensis is an N-formyltransferase that functions on dTDP-4-amino-4,6-dideoxy-d-glucose as its substrate. The enzyme, hereafter referred to as WbtJ, demonstrates a strict requirement for N(10) -formyltetrahydrofolate as its carbon source. In addition to the kinetic analysis, the three-dimensional structure of the enzyme was solved in the presence of dTDP-sugar ligands to a nominal resolution of 2.1 Å. Each subunit of the dimeric enzyme is dominated by a "core" domain defined by Met 1 to Ser 185. This core motif harbors the active site residues. Following the core domain, the last 56 residues fold into two α-helices and a β-hairpin motif. The hairpin motif is responsible primarily for the subunit:subunit interface, which is characterized by a rather hydrophobic pocket. From the study presented here, it is now known that WbtJ functions on C-4' amino sugars. Another enzyme recently investigated in the laboratory, WlaRD, formylates only C-3' amino sugars. Strikingly, the quaternary structures of WbtJ and WlaRD are remarkably different. In addition, there are several significant variations in the side chains that line their active site pockets, which may be important for substrate specificity. Details concerning the kinetic and structural properties of WbtJ are presented.
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