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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment
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Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment

机译：protease-cleaved大肠杆菌的结构alpha-2-macroglobulin揭示了一个假定的构象激活的机制蛋白酶截留

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摘要

Bacterial alpha-2-macroglobulins have been suggested to function in defence as broad-spectrum inhibitors of host proteases that breach the outer membrane. Here, the X-ray structure of protease-cleaved Escherichia coli alpha-2-macroglobulin is described, which reveals a putative mechanism of activation and conformational change essential for protease inhibition. In this competitive mechanism, protease cleavage of the bait-region domain results in the untethering of an intrinsically disordered region of this domain which disrupts native interdomain interactions that maintain E. coli alpha-2-macroglobulin in the inactivated form. The resulting global conformational change results in entrapment of the protease and activation of the thioester bond that covalently links to the attacking protease. Owing to the similarity in structure and domain architecture of Escherichia coli alpha-2-macroglobulin and human alpha-2-macroglobulin, this protease-activation mechanism is likely to operate across the diverse members of this group.
机译：细菌alpha-2-macroglobulins一直建议在防御功能广谱的宿主蛋白酶抑制剂违反外膜。protease-cleaved大肠杆菌的结构alpha-2-macroglobulin描述,揭示了一个假定的激活和机制构象变化必不可少的蛋白酶抑制。蛋白酶的乳沟bait-region域结果在本质上的“松绑”无序地区破坏的这个领域本机interdomain交互保持E。杆菌alpha-2-macroglobulin灭活的形式。诱捕的蛋白酶和结果激活的硫酯键共价链接到攻击蛋白酶。结构相似度和域架构大肠杆菌alpha-2-macroglobulin和人类alpha-2-macroglobulin,这protease-activation可能机制操作在不同的这一组的成员。

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