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 ¹H, ¹³C, ¹⁵N chemical shifts of WhiB4 protein in its reduced apo state, providing a basis for the determination of its solution structure.

WhiB4蛋白是WhiB样蛋白的一员，在结核分枝杆菌（ Mtb ）的生存和病理学中发挥着重要作用。作为一种转录因子，WhiB4 调节参与维持氧化还原稳态、中枢代谢和呼吸的基因的表达。此外，WhiB4 会导致分枝杆菌核仁的缩合，并能够与 DNA 结合。 WhiB4含有四个半胱氨酸残基，在不同的氧化还原环境下以多种形式存在，包括具有铁硫簇的二聚体完整形式、二硫键连接的多聚体氧化apo形式和单体还原apo形式。在这里，我们报告了WhiB4蛋白在还原apo状态下的¹ H、 ¹³ C、 ¹⁵ N化学位移，为其溶液结构的测定提供了基础。