Structure of the catalytic domain of the Salmonella virulence factor SseI

BhaskaranS.S.; StebbinsC.E.

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Structure of the catalytic domain of the Salmonella virulence factor SseI

机译：催化结构域的沙门氏菌毒力因子SseI

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SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 ? resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting of Cys178, His216 and Asp231 that is critical to its virulence activities. Structure-based analysis revealed that SseI is likely to possess either acyl hydrolase or acyltransferase activity, placing this virulence factor in the rapidly growing class of enzymes of this family utilized by bacterial pathogens inside eukaryotic cells.

机译：沙门氏菌和SseI分泌进入宿主细胞有助于建立系统性感染。1.70 c端SseI领域已经得到解决？半胱氨酸蛋白酶催化超科Cys178组成的三位一体,His216 Asp231其毒性活动至关重要。基于结构分析显示,SseI可能拥有或酰基水解酶酰基转移酶活性,这毒性因素迅速发展的一类酶这个家庭利用细菌病原体真核细胞内。

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《Acta crystallographica.Section D. Biological crystallography》 |2012年第12期|1613-1621|共9页
作者
BhaskaranS.S.; StebbinsC.E.;
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作者单位

Laboratory of Structural Microbiology, Rockefeller University, New York, NY 10065, United States;

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正文语种英语
中图分类化学;
关键词
Eukaryotic Cells; Catalytic Domain; crystal structureCysteine ProteasesSalmonellaVirulence FactorsNitric Oxide Synthase Type III;

机译：真核细胞;催化域;晶体FactorsNitric氧化合成酶类型III;

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Structure of the catalytic domain of the Salmonella virulence factor SseI

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