1H, 15N, 13C backbone resonance assignment of Escherichia coli AlkB in complex with Zn(II) and α-ketoglutarate

Protein and nucleic acid alkylation are important genetic and epigenetic modifications. The dynamic balance between alkylation and dealkylation is regulated by distinct sets of enzymes and is essential for maintaining genomic stability. Escherichia coli AlkB is a member of the Alkylation B (AlkB) family of dioxygenases that dealkylates a wide range of nucleic acid substrates in E. coli , thereby playing a crucial role in cellular repair processes and epigenetic regulation. Here, we report the backbone 1 H, 15 N, 13 C chemical shift assignment of E. coli AlkB in complex with Zn 2+ and α-ketoglutarate. Experiments were acquired at 20 °C by heteronuclear multidimensional NMR spectroscopy. Collectively, 91% of all 13 C, 15 N and 1 H backbone resonances of Alkb were assigned, with 182 out of a possible 200 residues assigned in the 1 H– 15 N TROSY spectrum. Using the program TALOS + , a secondary structure prediction was generated from the assigned backbone resonances that is consistent with the previously reported X-ray structure of the enzyme. The reported assignment will permit investigations of the protein structural dynamics anticipated to provide crucial insight regarding fundamental aspects in the recognition and enzyme regulation processes.