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

Authors

Sayan Das, Jeffrey A Purslow, Kyle Malcom, Joshua Knott, Vincenzo Venditti

Published in

Biomolecular NMR assignments. Volume 20. Issue 1. Jul 14, 2026. Epub Jul 14, 2026.

Abstract

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 ¹H, ¹⁵N, ¹³C chemical shift assignment of E. coli AlkB in complex with Zn²⁺ and α-ketoglutarate. Experiments were acquired at 20 °C by heteronuclear multidimensional NMR spectroscopy. Collectively, 91% of all ¹³C, ¹⁵N and ¹H backbone resonances of Alkb were assigned, with 182 out of a possible 200 residues assigned in the ¹H-¹⁵N 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.

PMID:
42446615
Bibliographic data and abstract were imported from PubMed on 14 Jul 2026.

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