NMR resonance assignments of NarE, a putative ADP-ribosylating toxin from Neisseria meningitidis |
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Authors: | Ludovic Carlier Christian Koehler Daniele Veggi Mariagrazia Pizza Marco Soriani Rolf Boelens Alexandre M. J. J. Bonvin |
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Affiliation: | (1) Bijvoet Center for Biomolecular Research, Science Faculty, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands;(2) Novartis Vaccines and Diagnostics, 53100 Siena, Italy;(3) Present address: Laboratoire des Biomol?cules, CNRS UMR7203, UPMC Universit? Paris 06, 75005 Paris, France; |
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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 15N- and 15N/13C-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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