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 )的存活和病理中起重要作用。作为转录因子，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 导致分枝杆菌核素的凝聚，并能够与 DNA 结合。WhiB4 包含四个半胱氨酸残基，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全息形式、多聚体二硫键连接的氧化 apo 形式和单体还原 apo 形式。在这里，我们报告了¹ H、¹³ C、¹⁵WhiB4 蛋白在还原 apo 状态下的 N 化学位移，为确定其溶液结构提供了基础。