ArticleBiochemistry2013
Structure of a sugar N-formyltransferase from Campylobacter jejuni.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Biodegradation of sulfonamide antibiotics by a soil bacteria enrichment and the impacts of soil organic matter.Eco-Environment & Health · 2026Article
- 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
- 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
- Modeling of interactions between functional domains of ALDH1L1.Chemico-biological interactions · 2017Article
- Biochemical Investigation of Rv3404c from Mycobacterium tuberculosis.Biochemistry · 2017Article
- Biochemical Characterization of WbkC, an N-Formyltransferase from Brucella melitensis.Biochemistry · 2017Article
- Characterization of the dTDP-Fuc3N and dTDP-Qui3N biosynthetic pathways in Campylobacter jejuni 81116.Glycobiology · 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
- Synthetic cycle of the initiation module of a formylating nonribosomal peptide synthetase.Nature · 2016Article
- 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
- Three-dimensional structure of a sugar N-formyltransferase from Francisella tularensis.Protein science : a publication of the Protein Society · 2014Article
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4 authors.
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Abstract
The O-antigens, which are components of the outer membranes of Gram-negative bacteria, are responsible for the wide species variations seen in nature and are thought to play a role in bacterial virulence. They often contain unusual dideoxysugars such as 3,6-dideoxy-3-formamido-d-glucose (Qui3NFo). Here, we describe a structural and functional investigation of the protein C8J_1081 from Campylobacter jejuni 81116, which is involved in the biosynthesis of Qui3NFo. Specifically, the enzyme, hereafter referred to as WlaRD, catalyzes the N-formylation of dTDP-3,6-dideoxy-3-amino-d-glucose (dTDP-Qui3N) using N(10)-formyltetrahydrofolate as the carbon source. For this investigation, seven X-ray structures of WlaRD, in complexes with various dTDP-linked sugars and cofactors, were determined to resolutions of 1.9 Å or better. One of the models, with bound N(10)-formyltetrahydrofolate and dTDP, represents the first glimpse of an N-formyltransferase with its natural cofactor. Another model contains the reaction products, tetrahydrofolate and dTDP-Qui3NFo. In combination, the structures provide snapshots of the WlaRD active site before and after catalysis. On the basis of these structures, three amino acid residues were targeted for study: Asn 94, His 96, and Asp 132. Mutations of any of these residues resulted in a complete loss of enzymatic activity. Given the position of His 96 in the active site, it can be postulated that it functions as the active site base to remove a proton from the sugar amino group as it attacks the carbonyl carbon of the N-10 formyl group of the cofactor. Enzyme assays demonstrate that WlaRD is also capable of utilizing dTDP-3,6-dideoxy-3-amino-d-galactose (dTDP-Fuc3N) as a substrate, albeit at a much reduced catalytic efficiency.
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