8ETD
Crystal Structure of Schizosaccharomyces pombe Rho1
Summary for 8ETD
| Entry DOI | 10.2210/pdb8etd/pdb |
| Descriptor | GTP-binding protein rho1, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | gtpase, rho, gdp, evolution, gene regulation |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
| Total number of polymer chains | 2 |
| Total formula weight | 46045.04 |
| Authors | Huang, Q.,Xie, J.,Seetharaman, J. (deposition date: 2022-10-16, release date: 2022-12-07, Last modification date: 2023-10-25) |
| Primary citation | Huang, Q.,Xie, J.,Seetharaman, J. Crystal Structure of Schizosaccharomyces pombe Rho1 Reveals Its Evolutionary Relationship with Other Rho GTPases. Biology (Basel), 11:-, 2022 Cited by PubMed Abstract: 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. PubMed: 36358328DOI: 10.3390/biology11111627 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.78 Å) |
Structure validation
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