Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase
Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase
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DOI：
10.1038/nsmb1346
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发表时间：
2008-01-01
影响因子：
16.8
通讯作者：
Chen, Jue
中科院分区：
文献类型：
--
作者：
Diao, Jianbo;Zhang, Ying;Chen, Jue
细菌病原体将毒力蛋白递送到宿主细胞中以促进进入和存活。沙门氏菌SopA作为E3连接酶发挥作用以操纵宿主促炎反应。在这里，我们报告的晶体结构的SOPA在两种构象。虽然它与真核HECT结构域E3的序列相似性很小，但SopA的C-末端一半具有双叶结构，这让人想起HECT结构域的N-和C-叶排列。SopA结构还含有一个假定的底物结合域，位于E2结合位点附近。这两种结构的SopA不同的C叶的相对取向，表明SopA具有构象的灵活性HECT E3功能必不可少。这些结果表明，SopA是一个独特的HECT E3连接酶进化的共进化选择压力在细菌-宿主界面。
Bacterial pathogens deliver virulence proteins into host cells to facilitate entry and survival. Salmonella SopA functions as an E3 ligase to manipulate the host proinflammatory response. Here we report the crystal structure of SopA in two conformations. Although it has little sequence similarity to eukaryotic HECT-domain E3s, the C-terminal half of SopA has a bilobal architecture that is reminiscent of the N- and C-lobe arrangement of HECT domains. The SopA structure also contains a putative substrate-binding domain located near the E2-binding site. The two structures of SopA differ in the relative orientations of the C lobe, indicating that SopA possesses the conformational flexibility essential for HECT E3 function. These results suggest that SopA is a unique HECT E3 ligase evolved from the coevolutionary selective pressure at the bacterium-host interface.