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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Purification, crystallization and preliminary X-ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA-I from Escherichia coli
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Purification, crystallization and preliminary X-ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA-I from Escherichia coli

机译：大肠杆菌单体自转运蛋白AIDA-I转运单元的纯化，结晶和初步X射线晶体学分析

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摘要

The adhesin involved in diffuse adherence (AIDA-I) from Escherichia coli belongs to the group of autotransporters, specifically the type Va secretion system (T5aSS). All autotransporter systems contain a C-terminal beta-domain, which forms a barrel-like structure in the outer membrane with a hydrophilic pore allowing passenger translocation across the outer membrane. The passenger domain harbours the biological activity in the extracellular space and functions, for example, as an adhesin, an enzyme and a toxin. The exact transport mechanism of passenger translocation across the outer membrane is not clear at present. Thus, structure determination of the transport unit of AIDA-I could provide new insights into the transport mechanism. Here, the purification, crystallization and preliminary X-ray crystallographic studies of the transport unit of AIDA-I are reported.
机译：与大肠杆菌的弥散性粘附有关的粘附素（AIDA-1）属于自转运蛋白，特别是Va分泌系统（T5aSS）。所有的自动转运蛋白系统都包含一个C端β结构域，该结构域在外膜中形成一个桶状结构，并带有一个亲水孔，从而允许乘客跨过外膜进行转运。客运域在细胞外空间中具有生物活性并具有例如作为粘附素，酶和毒素的功能。目前尚不清楚乘客穿越外膜的确切运输机制。因此，确定AIDA-1的运输单元的结构可以为运输机制提供新的见解。在此，报道了AIDA-1转运单元的纯化，结晶和初步X射线晶体学研究。

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