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<p>The Alkbh7 protein, a member of the Alkylation B (AlkB) family of dioxygenases, plays a crucial role in epigenetic regulation of cellular metabolism. This paper focuses on the NMR backbone resonance assignment of Alkbh7, a fundamental step in understanding its three-dimensional structure and dynamic behavior at the atomic level. Herein, we report the backbone <sup>1</sup>H, <sup>15</sup>N, <sup>13</sup>C chemical shift assignment of the full-length human Alkbh7. Experiments were acquired at 25&#xa0;°C by heteronuclear multidimensional NMR spectroscopy. Collectively, 70% of the backbone NH resonances were assigned, with 144 out of a possible 205 residues assigned in the <sup>1</sup>H-<sup>15</sup>N TROSY spectrum. Interestingly, peaks from the active site and the C-terminal end of Alkbh7 are not NMR visible, suggesting that these regions are dynamic on the intermediate exchange regime. Using the program TALOS+, a secondary structure prediction was generated from the assigned backbone resonance 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.</p>

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1H, 15N, 13C backbone resonance assignment of human Alkbh7

  • 期刊论文

  • 发表日期：

    2025年1月29日

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  • Baboucarr Faal,
  • Jeffrey A. Purslow,
  • Vincenzo Venditti

摘要

The Alkbh7 protein, a member of the Alkylation B (AlkB) family of dioxygenases, plays a crucial role in epigenetic regulation of cellular metabolism. This paper focuses on the NMR backbone resonance assignment of Alkbh7, a fundamental step in understanding its three-dimensional structure and dynamic behavior at the atomic level. Herein, we report the backbone 1H, 15N, 13C chemical shift assignment of the full-length human Alkbh7. Experiments were acquired at 25 °C by heteronuclear multidimensional NMR spectroscopy. Collectively, 70% of the backbone NH resonances were assigned, with 144 out of a possible 205 residues assigned in the 1H-15N TROSY spectrum. Interestingly, peaks from the active site and the C-terminal end of Alkbh7 are not NMR visible, suggesting that these regions are dynamic on the intermediate exchange regime. Using the program TALOS+, a secondary structure prediction was generated from the assigned backbone resonance 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.