ArticlePloS one2011
Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Sialic acid O-acetylation: From biosynthesis to roles in health and disease.The Journal of biological chemistry · 2021Review
- Chemical structure and genetic organization of the E. coli O6:K15 capsular polysaccharide.Scientific reports · 2020Article
- An enzyme-based protocol for cell-free synthesis of nature-identical capsular oligosaccharides fromThe Journal of biological chemistry · 2020Article
- Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA).Acta crystallographica. Section D, Biological crystallography · 2015Article
- Functions and Biosynthesis of O-Acetylated Sialic Acids.Topics in current chemistry · 2015Review
- Masquerading microbial pathogens: capsular polysaccharides mimic host-tissue molecules.FEMS microbiology reviews · 2014Review
- Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly.The Journal of biological chemistry · 2012Article
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Authors and funding
4 authors.
Funding
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Abstract
The major virulence factor of the neuroinvasive pathogen Escherichia coli K1 is the K1 capsule composed of α2,8-linked polysialic acid (polySia). K1 strains harboring the CUS-3 prophage modify their capsular polysaccharide by phase-variable O-acetylation, a step that is associated with increased virulence. Here we present the crystal structure of the prophage-encoded polysialate O-acetyltransferase NeuO. The homotrimeric enzyme belongs to the left-handed β-helix (LβH) family of acyltransferases and is characterized by an unusual funnel-shaped outline. Comparison with other members of the LβH family allowed the identification of active site residues and proposal of a catalytic mechanism and highlighted structural characteristics of polySia specific O-acetyltransferases. As a unique feature of NeuO, the enzymatic activity linearly increases with the length of the N-terminal poly-ψ-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad. Since the poly-ψ-domain was not resolved in the crystal structure it is assumed to be unfolded in the apo-enzyme.
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