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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the nucleotide-binding domain of Plasmodium falciparum Rab6 in the GDP-bound form
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Structure of the nucleotide-binding domain of Plasmodium falciparum Rab6 in the GDP-bound form

机译：nucleotide-binding结构域的恶性疟原虫Rab6蛋白的形式

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摘要

Rab proteins are small Ras-like GTPases which play important roles in regulating intracellular vesicle trafficking. The nucleotide-binding domain of Rab6 from the malaria parasite Plasmodium falciparum was crystallized with GDP bound to the active site. The MAD phasing technique was used to determine the crystal structure to 2.3 A resolution. Comparisons of the structure of GDP-bound PfRab6 with the recently determined structures of Rab3A in complex with either a GTP analog or with GTP and Rabphillin present structural evidence supporting the traditional model for the molecular GTP/GDP switch in Rab proteins. PfRab6 residues homologous to those distinguishing human Rab6 isoforms, which differ in binding to Rabkinesin-6 in human cells, are located next to the recognized complementarity-determining region (CDR) and constitute a conceptual broadening of that domain. Despite significant observable differences in Golgi ultrastructure, the Rab6 core structure and switch mechanism appear highly conserved when compared with murine Rab3a structures. A significant difference between the PfRab6 and higher eukaryotic Rabs may be the lack of CDR features that allow binding interactions with Rabkinesin-type effectors.
机译：Rab蛋白质小Ras-like gtpase玩在调节细胞内的重要作用泡贩运。域的Rab6疟疾寄生虫恶性疟原虫与GDP的结晶绑定到活性部位。技术被用来确定晶体2.3结构解析。结构蛋白PfRab6最近Rab3A在复杂结构决定的三磷酸鸟苷模拟或三磷酸鸟苷和Rabphillin提供结构性的证据支持传统的模型分子三磷酸鸟苷/ GDP开关在Rab蛋白质。人类Rab6同源的区别不同亚型,Rabkinesin-6绑定在人类细胞,位于旁边承认complementarity-determining地区(CDR)和构成的概念扩大该域。Rab6高尔基体超微结构的差异核心结构和开关机制出现高度守恒与小鼠Rab3a相比结构。PfRab6和高等真核rab可能缺乏CDR的特性,允许绑定交互Rabkinesin-type效应器。

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