1XO3
Solution Structure of Ubiquitin like protein from Mus Musculus
Summary for 1XO3
| Entry DOI | 10.2210/pdb1xo3/pdb |
| NMR Information | BMRB: 6337 |
| Descriptor | RIKEN cDNA 2900073H19 (1 entity in total) |
| Functional Keywords | structural genomics, protein structure initiative, center for eukaryotic structural genomics, psi, cesg, unknown function |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm (By similarity): Q9D2P4 |
| Total number of polymer chains | 1 |
| Total formula weight | 11289.90 |
| Authors | Singh, S.,Tonelli, M.,Tyler, R.C.,Bahrami, A.,Lee, M.S.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-10-05, release date: 2004-10-19, Last modification date: 2024-05-22) |
| Primary citation | Singh, S.,Tonelli, M.,Tyler, R.C.,Bahrami, A.,Lee, M.S.,Markley, J.L. Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1. Protein Sci., 14:2095-2102, 2005 Cited by PubMed Abstract: We have used NMR spectroscopy to determine the solution structure of protein AAH26994.1 from Mus musculus and propose that it represents the first three-dimensional structure of a ubiquitin-related modifier 1 (Urm1) protein. Amino acid sequence comparisons indicate that AAH26994.1 belongs to the Urm1 family of ubiquitin-like modifier proteins. The best characterized member of this family has been shown to be involved in nutrient sensing, invasive growth, and budding in yeast. Proteins in this family have only a weak sequence similarity to ubiquitin, and the structure of AAH26994.1 showed a much closer resemblance to MoaD subunits of molybdopterin synthases (known structures are of three bacterial MoaD proteins with 14%-26% sequence identity to AAH26994.1). The structures of AAH26994.1 and the MoaD proteins each contain the signature ubiquitin secondary structure fold, but all differ from ubiquitin largely in regions outside of this fold. This structural similarity bolsters the hypothesis that ubiquitin and ubiquitin-related proteins evolved from a protein-based sulfide donor system of the molybdopterin synthase type. PubMed: 16046629DOI: 10.1110/ps.051577605 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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