Structural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility-mass spectrometry
Structural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility-mass spectrometry
复制标题
DOI：
10.1042/bcj20190318
复制
发表时间：
2019-11-01
影响因子：
4.1
通讯作者：
Abell, Chris
中科院分区：
文献类型：
--
作者：
Chan, Daniel Shiu-Hin;Hess, Jeannine;Abell, Chris
CoaBC是细菌中重要的辅酶A生物合成途径的一部分，最近已被验证为有前途的抗菌靶标。在这项工作中，我们采用自然离子迁移率质谱法获得的磷酸泛噻吩甲酰半胱氨酸合成酶结构域的E。coli CoaBC.此外，原生质谱法被验证为筛选工具，以确定这种酶的新型抑制剂，突出了这种技术的结构生物学和药物发现的实用性和多功能性。
CoaBC, part of the vital coenzyme A biosynthetic pathway in bacteria, has recently been validated as a promising antimicrobial target. In this work, we employed native ion mobility-mass spectrometry to gain structural insights into the phosphopantothenoylcysteine synthetase domain of E. coli CoaBC. Moreover, native mass spectrometry was validated as a screening tool to identify novel inhibitors of this enzyme, highlighting the utility and versatility of this technique both for structural biology and for drug discovery.