ArticleProtein science : a publication of the Protein Society2016
Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N(5) -formyltetrahydrofolate and UDP-Ara4N.
Article in Protein science : a publication of the Protein Society, 2016. 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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8 citing papers in PubMed.
- Structural basis of undecaprenyl phosphate glycosylation leading to polymyxin resistance in Gram-negative bacteria.Nature communications · 2025Article
- Structural Basis for Targeting the Bifunctional Enzyme ArnA.Biomolecules · 2025Article
- 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
- 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
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Abstract
ArnA from Escherichia coli is a key enzyme involved in the formation of 4-amino-4-deoxy-l-arabinose. The addition of this sugar to the lipid A moiety of the lipopolysaccharide of pathogenic Gram-negative bacteria allows these organisms to evade the cationic antimicrobial peptides of the host immune system. Indeed, it is thought that such modifications may be responsible for the repeated infections of cystic fibrosis patients with Pseudomonas aeruginosa. ArnA is a bifunctional enzyme with the N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively. The catalytically competent cofactor for the formylation reaction is N(10) -formyltetrahydrofolate. Here we describe the structure of the isolated N-terminal domain of ArnA in complex with its UDP-sugar substrate and N(5) -formyltetrahydrofolate. The model presented herein may prove valuable in the development of new antimicrobial therapeutics.
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