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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body.
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A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body.

机译：一个保守域III型分泌链接胞质域再次的元素基体。

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摘要

Protein type III secretion systems (T3SSs) are organic nanosyringes that achieve an energy-dependent translocation of bacterial proteins through the two membranes of Gram-negative organisms. Examples include the pathogenic systems of animals, plants and symbiotic bacteria that inject factors into eukaryotic cells, and the flagellar export system that secretes flagellin. T3SSs possess a core of several membrane-associated proteins that are conserved across all known bacterial species that use this system. The Salmonella protein InvA is one of the most highly conserved proteins of this core of critical T3SS components. The crystal structure of a C-terminal domain of InvA reveals an unexpected homology to domains that have been repeatedly found as building blocks of other elements of the T3SS apparatus. This suggests the surprising hypothesis that evolution has produced a significant component of the apparatus structure through a series of gene-duplication and gene-rearrangement events.
机译：蛋白质III型分泌系统(T3SSs)有机nanosyringes实现一个依赖资源的细菌易位通过的两个膜蛋白革兰氏阴性细菌。致病性系统的动物、植物共生细菌注入因素真核细胞,鞭毛出口体系分泌鞭毛蛋白。几个膜相关蛋白保存所有已知的细菌物种使用这个系统。的高度保守的蛋白质的核心关键T3SS组件。再次显示c端结构域一个意想不到的相同的域多次发现作为构建块的元素T3SS装置。惊人的假说,进化产生了装置的重要组成部分通过一系列的重复基因结构和基因重排事件。

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