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Unraveling the mechanism of peptidoglycan amidation by the bifunctional enzyme complex GatD/MurT: A comparative structural approach.
International Journal of Medical Microbiology ( IF 4.5 ) Pub Date : 2019-07-18 , DOI: 10.1016/j.ijmm.2019.151334
Erik R Nöldeke 1 , Thilo Stehle 2
Affiliation  

The bacterial cell wall provides structural integrity to the cell and protects the cell from internal pressure and the external environment. During the course of the twelve-year funding period of the Collaborative Research Center 766, our work has focused on conducting structure-function studies of enzymes that modify (synthesize or cleave) cell wall components of a range of bacteria including Staphylococcus aureus, Staphylococcus epidermidis, and Nostoc punctiforme. Several of our structures represent promising targets for interference. In this review, we highlight a recent structure-function analysis of an enzyme complex that is responsible for the amidation of Lipid II, a peptidoglycan precursor, in S. aureus.



中文翻译:

通过双功能酶复合物GatD / MurT揭示肽聚糖酰胺化的机理:一种比较结构方法。

细菌细胞壁为细胞提供结构完整性,并保护细胞免受内部压力和外部环境的影响。在766协作研究中心的十二年资助期间,我们的工作重点是进行修饰(合成或切割)包括金黄色葡萄球菌表皮葡萄球菌在内的多种细菌的细胞壁成分的酶的结构功能研究。和点状鼻头虫。我们的几个结构代表了有希望的干扰目标。在这篇综述中,我们重点介绍了一种酶复合物的近期结构-功能分析,该酶复合物负责金黄色葡萄球菌脂肽II(一种肽聚糖前体)的酰胺化。

更新日期:2019-07-18
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