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.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9687936 | PMC |
http://dx.doi.org/10.3390/biology11111627 | DOI Listing |
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