Huang Qingqing, Xie Jiarong, Seetharaman Jayaraman
Department of Biological Sciences, 14 Science Drive 4, National University of Singapore, Singapore 117543, Singapore.
Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Biology (Basel). 2022 Nov 7;11(11):1627. doi: 10.3390/biology11111627.
The Rho protein, a homolog of Ras, is a member of the Ras superfamily of small GTPases. Rho family proteins are involved in cytoskeletal organization, cell mobility, and polarity, and are implicated in cancer morphogenesis. Although Rho homologs from higher-order mammalian organisms are well studied, there are few studies examining Rho proteins in lower-level single-celled organisms. Here, we report on the crystal structure of Rho1 from (Rho1) in complex with GDP in the presence of Mg at a 2.78 Å resolution. The overall structure is similar to that of known Rho homologs, including human RhoA, human RhoC, and Rho1 (Rho1), with some exceptions. We observed subtle differences at the Switch I and II regions, in β2 and β3, and in the Rho insert domain and loop from Phe107 to Pro112. Our analysis suggests that Rho is evolutionarily closer to RhoC than RhoA, as previously believed.
Rho蛋白是Ras的同源物，属于小GTP酶的Ras超家族成员。Rho家族蛋白参与细胞骨架组织、细胞迁移和极性形成，并与癌症形态发生有关。尽管来自高等哺乳动物的Rho同源物已得到充分研究，但对低等单细胞生物中的Rho蛋白研究较少。在此，我们报道了在存在镁离子的情况下，Rho1与GDP复合物的晶体结构，分辨率为2.78Å。其整体结构与已知的Rho同源物相似，包括人RhoA、人RhoC和Rho1，但也有一些例外。我们在开关I和II区域、β2和β3以及Rho插入结构域和从苯丙氨酸107到脯氨酸112的环处观察到细微差异。我们的分析表明，Rho在进化上比之前认为的更接近RhoC，而不是RhoA。
