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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >IpaB-IpgC interaction defines binding motif for type Ⅲ secretion translocator
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IpaB-IpgC interaction defines binding motif for type Ⅲ secretion translocator

机译:IpaB-IpgC相互作用定义了Ⅲ型分泌转运蛋白的结合基序

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摘要

The delivery of virulence factors into host cells through type Ⅲ secretion systems is essential for enterobacterial pathogenesis. Molecular chaperones bind specifically to virulence factors in the bacterial cytosol before secretion. Invasion plasmid gene C (IpgC) is a chaperone that binds 2 essential virulence factors of Shigella: invasion plasmid antigens (Ipa) B and C. Here, we report the crystal structure of IpgC alone and in complex with the chaperone binding domain (CBD) of IpaB. The chaperone captures the CBD in an extended conformation that is stabilized by conserved residues lining the cleft. Analysis of the cocrystal structure reveals a sequence motif that is functional in the IpaB translocator class from different bacteria as determined by isothermal titration calorime-try. Our results show how translocators are chaperoned and may allow the design of inhibitors of enterobacterial diseases.
机译:通过Ⅲ型分泌系统将毒力因子传递到宿主细胞中对于肠道细菌的发病机理至关重要。分子伴侣在分泌前特异性结合细菌细胞质中的毒力因子。侵袭质粒基因C(IpgC)是一种结合志贺氏菌2个基本毒力因子的伴侣蛋白:侵袭质粒抗原(Ipa)B和C。在这里,我们报道了IpgC的晶体结构,并且与伴侣结合结构域(CBD)复杂IpaB。分子伴侣以扩展的构象捕获CBD,该构象通过裂口内的保守残基稳定。对共晶体结构的分析揭示了一个序列基序,该序列基序在等温滴定量热法测定的不同细菌的IpaB易位子类别中起作用。我们的研究结果表明易位分子是如何被伴侣化的,并且可能允许设计肠细菌性疾病的抑制剂。

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