1H, 13C, and 15N resonance assignments of reduced apo-WhiB4 from Mycobacterium tuberculosis

The WhiB4 protein, a member of WhiB-like proteins, plays an important role in the survival and pathology of Mycobacterium tuberculosis (Mtb). As a transcription factor, WhiB4 regulates the expression of genes involved in maintaining redox homeostasis, central metabolism, and respiration. Furthermore, WhiB4 leads to the condensation of mycobacterial nucleoids and is capable of binding to DNA. WhiB4 contains four cysteine residues and exists in multiple forms under different redox environments, including a dimeric holo form with iron-sulfur cluster, multimeric disulfide-linked oxidized apo forms and monomeric reduced apo form. Here, we report the H-1, C-13, N-15 chemical shifts of WhiB4 protein in its reduced apo state, providing a basis for the determination of its solution structure.

Automated summary

WhiB4 protein, a member of the WhiB-like protein family, plays a crucial role in the survival and pathology of Mycobacterium tuberculosis. Acting as a transcription factor, WhiB4 regulates genes involved in redox balance, central metabolism, and respiration. It exists in different forms under different redox environments, including a dimeric holo form with iron-sulfur cluster, multimeric disulfide-linked oxidized apo forms, and a monomeric reduced apo form.