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首页> 外文期刊>Acta crystallographica.Section D Biological crystallography. >Structural and enzymatic characterization of a host-specificity determinant from Salmonella
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Structural and enzymatic characterization of a host-specificity determinant from Salmonella

机译:结构和酶的特性微型行列式的沙门氏菌

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摘要

GtgE is an effector protein from Salmonella Typhimurium that modulates trafficking of the Salmonella-containing vacuole. It exerts its function by cleaving the Rab-family GTPases Rab29, Rab32 and Rab38, thereby preventing the delivery of antimicrobial factors to the bacteria-containing vacuole. Here, the crystal structure of GtgE at 1.65 ? resolution is presented, and structure-based mutagenesis and in vivo infection assays are used to identify its catalytic triad. A panel of cysteine protease inhibitors were examined and it was determined that N-ethylmaleimide, antipain and chymostatin inhibit GtgE activity in vitro. These findings provide the basis for the development of novel therapeutic strategies to combat Salmonella infections.
机译:GtgE沙门氏菌是一种效应蛋白沙门氏菌感染,调节贩卖的Salmonella-containing液泡。函数通过裂开Rab-family gtpaseRab29, Rab32 Rab38,从而阻止了交付的抗菌因子bacteria-containing液泡。在1.65 GtgE结构吗?,并给出了基于结构突变和分析用来确定其体内感染催化三和弦。抑制剂进行确定N-ethylmaleimide, antipain chymostatin在体外抑制GtgE活动。小说的发展提供了依据治疗策略应对沙门氏菌感染。

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