NMR resonance assignments of NarE, a putative ADP-ribosylating toxin from Neisseria meningitidis.
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.
Carlier
Ludovic
L
Bijvoet Center for Biomolecular Research, Science Faculty, Utrecht University, The Netherlands.
Koehler
Christian
C
Veggi
Daniele
D
Pizza
Mariagrazia
M
Soriani
Marco
M
Boelens
Rolf
R
Bonvin
Alexandre M J J
AM
D036002:ADP Ribose Transferases / Q000737:chemistry*; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000595:Amino Acid Sequence; D001427:Bacterial Toxins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
D001427:Bacterial Toxins; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases; C480854:NarE protein, Neisseria meningitidis