3CMM
Crystal Structure of the Uba1-Ubiquitin Complex
Summary for 3CMM
| Entry DOI | 10.2210/pdb3cmm/pdb |
| Descriptor | Ubiquitin-activating enzyme E1 1, Ubiquitin, PROLINE, ... (4 entities in total) |
| Functional Keywords | ubiquitin, e1, uba1, protein turnover, ligase, conformational change, thioester, adenylation, transthioesterification, atp-binding, nucleotide-binding, nucleus, phosphoprotein, ubl conjugation pathway, dna damage, dna repair, ligase-protein binding complex, ligase/protein binding |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Cytoplasm: P22515 |
| Total number of polymer chains | 4 |
| Total formula weight | 244399.75 |
| Authors | Lee, I.,Schindelin, H. (deposition date: 2008-03-23, release date: 2008-08-05, Last modification date: 2024-02-21) |
| Primary citation | Lee, I.,Schindelin, H. Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes. Cell(Cambridge,Mass.), 134:268-278, 2008 Cited by PubMed Abstract: Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their targets by specific cascades involving three classes of enzymes, E1, E2, and E3. Each E1 adenylates the C terminus of its cognate Ubl, forms a E1 approximately Ubl thioester intermediate, and ultimately generates a thioester-linked E2 approximately Ubl product. We have determined the crystal structure of yeast Uba1, revealing a modular architecture with individual domains primarily mediating these specific activities. The negatively charged C-terminal ubiquitin-fold domain (UFD) is primed for binding of E2s and recognizes their positively charged first alpha helix via electrostatic interactions. In addition, a mobile loop from the domain harboring the E1 catalytic cysteine contributes to E2 binding. Significant, experimentally observed motions in the UFD around a hinge in the linker connecting this domain to the rest of the enzyme suggest a conformation-dependent mechanism for the transthioesterification function of Uba1; however, this mechanism clearly differs from that of other E1 enzymes. PubMed: 18662542DOI: 10.1016/j.cell.2008.05.046 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
