蛋白质酪氨酸磷酸酶
磷酸酶
半胱氨酸
双特异性磷酸酶
结核分枝杆菌
磷酸化
生物化学
毒力因子
酪氨酸
DUSP6型
酪氨酸磷酸化
蛋白磷酸酶2
化学
毒力
细胞生物学
酶
生物
肺结核
基因
医学
病理
作者
Anna Niesteruk,Sridhar Sreeramulu,Hendrik R. A. Jonker,Christian Richter,Harald Schwalbe
出处
期刊:FEBS Letters
[Wiley]
日期:2022-04-15
卷期号:596 (12): 1503-1515
被引量:1
标识
DOI:10.1002/1873-3468.14348
摘要
The Mycobacterium tuberculosis tyrosine-specific phosphatase MptpA and its cognate kinase PtkA are prospective targets for anti-tuberculosis drugs as they interact with the host defense response within the macrophages. Although both are structurally well-characterized, the functional mechanism regulating their activity remains poorly understood. Here, we investigate the effect of post-translational oxidation in regulating the function of MptpA. Treatment of MptpA with H2 O2 /NaHCO3 , mimicking cellular oxidative stress conditions, leads to oxidation of the catalytic cysteine (C11) and to a conformational rearrangement of the phosphorylation loop (D-loop) by repositioning the conserved tyrosine 128 (Y128) and generating a temporarily inactive preclosed state of the phosphatase. Thus, the catalytic cysteine in the P-loop acts as a redox switch and regulates the phosphatase activity of MptpA.
科研通智能强力驱动
Strongly Powered by AbleSci AI