Scaffold modules known as aminoacyl‐tRNA synthetase (aaRS)‐interacting multifunctional proteins (AIMPs), such as AIMP1/p43, AIMP2/p38 and AIMP3/p18, are important in driving the assembly of multi‐aaRS (MARS) complexes in eukaryotes. Often, AIMPs contain an N‐terminal glutathione S‐transferase (GST)‐like domain and a C‐terminal OB‐fold tRNA‐binding domain. Recently, the apicomplexan‐specific Plasmodium falciparum p43 protein (Pfp43) has been annotated as an AIMP and its tRNA binding, tRNA import and membrane association have been characterized. The crystal structures of both the N‐ and C‐terminal domains of the Plasmodium vivax p43 protein (Pvp43), which is an ortholog of Pfp43, have been resolved. Analyses reveal the overall oligomeric structure of Pvp43 and highlight several notable features that show Pvp43 to be a soluble, cytosolic protein. The dimeric assembly of the N‐terminal GST‐like domain of Pvp43 differs significantly from canonical GST dimers, and it is tied to the C‐terminal tRNA‐binding domain via a linker region. This work therefore establishes a framework for dissecting the additional roles of p43 orthologs in eukaryotic multi‐protein MARS complexes.

中文翻译：

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构成间日疟原虫p43蛋白的两个域的晶体结构。

称为氨酰基-tRNA合成酶（aaRS）相互作用多功能蛋白（AIMP）的支架模块，如AIMP1 / p43，AIMP2 / p38和AIMP3 / p18，在驱动真核生物中的multi-aaRS（MARS）复合体组装中很重要。AIMP通常包含一个N端谷胱甘肽S转移酶（GST）样结构域和一个C端OB折叠tRNA结合结构域。最近，已将apicomplexan特异的恶性疟原虫p43蛋白（Pf p43）注释为AIMP，并对其tRNA结合，tRNA导入和膜缔合进行了表征。间日疟原虫p43蛋白（Pv p43）的N和C端结构域的晶体结构，这是Pf的直系同源物p43，已经解决。分析揭示了Pv p43的整体寡聚结构，并突出了几个显着特征，这些特征表明Pv p43是一种可溶性胞质蛋白。Pv p43的N末端GST样结构域的二聚体组装与典型的GST二聚体显着不同，并且它通过接头区域与C末端tRNA结合域相连。因此，这项工作建立了一个框架，用于剖析p43直系同源物在真核多蛋白MARS复合物中的其他作用。