Carlier Ludovic, Koehler Christian, Veggi Daniele, Pizza Mariagrazia, Soriani Marco, Boelens Rolf, Bonvin Alexandre M J J
Bijvoet Center for Biomolecular Research, Science Faculty, Utrecht University, The Netherlands.
Biomol NMR Assign. 2011 Apr;5(1):35-8. doi: 10.1007/s12104-010-9261-6. Epub 2010 Aug 25.
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.
NarE是一种从脑膜炎奈瑟菌中鉴定出的16 kDa蛋白质，脑膜炎奈瑟菌是引起脑膜炎的细菌病原体之一。NarE属于ADP核糖基转移酶家族，催化ADP核糖部分转移到靶蛋白受体中的精氨酸残基上。许多致病细菌利用ADP核糖基化毒素来修饰和改变真核细胞的基本功能。有人提出NarE通过一个铁硫中心结合铁，该铁硫中心被认为参与催化过程。我们制备并纯化了均匀标记的（15）N-和（15）N/（13）C-NarE，并使用多维异核NMR光谱确定了主链和侧链共振。这些归属为NarE的三维结构测定以及铁硫中心在催化机制中的作用表征提供了起点。
