ArticleBiomolecular NMR assignments2011
NMR resonance assignments of NarE, a putative ADP-ribosylating toxin from Neisseria meningitidis.
Article in Biomolecular NMR assignments, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Targeting ADP-ribosylation as an antimicrobial strategy.Biochemical pharmacology · 2019Review
- Structural and biochemical characterization of NarE, an iron-containing ADP-ribosyltransferase from Neisseria meningitidis.The Journal of biological chemistry · 2011Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
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Abstract
NarE is a 16 kDa protein identified from Neisseria meningitidis, one of the bacterial pathogens responsible for meningitis. NarE belongs to the ADP-ribosyltransferase family and catalyses the transfer of ADP-ribose moieties to arginine residues in target protein acceptors. Many pathogenic bacteria utilize ADP-ribosylating toxins to modify and alter essential functions of eukaryotic cells. NarE was proposed to bind iron through a Fe-S center which is supposed to be implied in catalysis. We have produced and purified uniformly labeled (15)N- and (15)N/(13)C-NarE and assigned backbone and side-chain resonances using multidimensional heteronuclear NMR spectroscopy. These assignments provide the starting point for the three-dimensional structure determination of NarE and the characterization of the role of the Fe-S center in the catalytic mechanism.
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