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Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions

机译:两种细菌HECT样E3连接酶与人E2的晶体结构揭示了病原体与宿主相互作用的原子细节

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摘要

In eukaryotes, ubiquitination is an important posttranslational process achieved through a cascade of ubiquitin-activating (E1), conjugating (E2), and ligase (E3) enzymes. Many pathogenic bacteria deliver virulence factors into the host cell that function as E3 ligases. How these bacterial “Trojan horses” integrate into the eukaryotic ubiquitin system has remained a mystery. Here we report crystal structures of two bacterial E3s, Salmonella SopA and Escherichia coli NleL, both in complex with human E2 UbcH7. These structures represent two distinct conformational states of the bacterial E3s, supporting the necessary structural rearrangements associated with ubiquitin transfer. The E2-interacting surface of SopA and NleL has little similarity to those of eukaryotic E3s. However, both bacterial E3s bind to the canonical surface of E2 that normally interacts with eukaryotic E3s. Furthermore, we show that a glutamate residue on E3 is involved in catalyzing ubiquitin transfer from E3 to the substrate, but not from E2 to E3. Together, these results provide mechanistic insights into the ubiquitin pathway and a framework for understanding molecular mimicry in bacterial pathogenesis.
机译:在真核生物中,泛素化是通过泛素激活(E1),结合(E2)和连接酶(E3)的级联反应实现的重要翻译后过程。许多致病细菌将毒力因子传递到宿主细胞中,充当E3连接酶。这些细菌“特洛伊木马”如何整合到真核遍在蛋白系统中仍是一个谜。在这里,我们报告两个细菌E3的晶体结构,沙门氏菌SopA和大肠杆菌NleL,都与人E2 UbcH7形成复合体。这些结构代表细菌E3的两个不同的构象状态,支持与遍在蛋白转移相关的必要结构重排。 SopA和NleL的E2相互作用表面与真核E3几乎没有相似性。但是,两个细菌E3都与正常与真核E3相互作用的E2的规范表面结合。此外,我们表明,E3上的谷氨酸残基参与催化泛素从E3转移至底物,但不从E2转移至E3。综合起来,这些结果为泛素途径提供了机械学见识,并为理解细菌发病机理中的分子模拟提供了框架。

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