Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector.

Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector.
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DOI:
10.1016/j.chom.2011.10.013
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发表时间:
2011-12-15
影响因子:
30.3
通讯作者:
Chai J
Chai J
中科院分区:
医学1区
文献类型:
--
作者:
Cheng W;Munkvold KR;Gao H;Mathieu J;Schwizer S;Wang S;Yan YB;Wang J;Martin GB;Chai J

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为了侵染植物,假单胞菌pv.番茄将约30种III型效应蛋白递送到宿主细胞中,其中许多干扰PAMP触发的免疫(PTI)。一种效应子AvrPtoB使用中央结构域结合宿主BAK 1来抑制PTI,BAK 1是一种与几种模式识别受体作用以激活防御信号的激酶。第二AvrPtoB结构域结合并抑制PTI相关激酶Bti 9,但相反地被蛋白激酶Pto识别以激活效应子触发的免疫。我们报告的晶体结构的AvrPtoB-BAK 1复合物,揭示了这两个AvrPtoB域之间的结构相似性,这表明它们产生的基因内复制。BAK 1激酶结构域在结构上类似于Pto,并且BAK 1和Pto内的保守区域与AvrPtoB相互作用。BAK 1激酶活性被AvrPtoB抑制,相互作用界面的突变破坏AvrPtoB毒力活性。这些结果揭示了宿主-病原体协同进化的结构机制。
To infect plants, Pseudomonas syringae pv. tomato delivers ~30 type III effector proteins into host cells, many of which interfere with PAMP-triggered immunity (PTI). One effector, AvrPtoB, suppresses PTI using a central domain to bind host BAK1, a kinase that acts with several pattern recognition receptors to activate defense signaling. A second AvrPtoB domain binds and suppresses the PTI-associated kinase Bti9 but is conversely recognized by the protein kinase Pto to activate effector-triggered immunity. We report the crystal structure of the AvrPtoB-BAK1 complex, which revealed structural similarity between these two AvrPtoB domains, suggesting that they arose by intragenic duplication. The BAK1 kinase domain is structurally similar to Pto, and a conserved region within both BAK1 and Pto interacts with AvrPtoB. BAK1 kinase activity is inhibited by AvrPtoB, and mutations at the interaction interface disrupt AvrPtoB virulence activity. These results shed light on a structural mechanism underlying host-pathogen coevolution.
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