1U9B
MURINE/HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9
Summary for 1U9B
| Entry DOI | 10.2210/pdb1u9b/pdb |
| Descriptor | UBIQUITIN-CONJUGATING ENZYME E9 (2 entities in total) |
| Functional Keywords | ubiquitin-conjugating enzyme, ubiquitin-directed proteolysis, cell cycle control, ligase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: P63280 |
| Total number of polymer chains | 1 |
| Total formula weight | 18258.08 |
| Authors | Tong, H.,Hateboer, G.,Perrakis, A.,Bernards, R.,Sixma, T.K. (deposition date: 1997-05-20, release date: 1997-07-07, Last modification date: 2024-05-22) |
| Primary citation | Tong, H.,Hateboer, G.,Perrakis, A.,Bernards, R.,Sixma, T.K. Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system. J.Biol.Chem., 272:21381-21387, 1997 Cited by PubMed Abstract: Murine/human ubiquitin-conjugating enzyme Ubc9 is a functional homolog of Saccharomyces cerevisiae Ubc9 that is essential for the viability of yeast cells with a specific role in the G2-M transition of the cell cycle. The structure of recombinant mammalian Ubc9 has been determined from two crystal forms at 2.0 A resolution. Like Arabidopsis thaliana Ubc1 and S. cerevisiae Ubc4, murine/human Ubc9 was crystallized as a monomer, suggesting that previously reported hetero- and homo-interactions among Ubcs may be relatively weak or indirect. Compared with the known crystal structures of Ubc1 and Ubc4, which regulate different cellular processes, Ubc9 has a 5-residue insertion that forms a very exposed tight beta-hairpin and a 2-residue insertion that forms a bulge in a loop close to the active site. Mammalian Ubc9 also possesses a distinct electrostatic potential distribution that may provide possible clues to its remarkable ability to interact with other proteins. The 2-residue insertion and other sequence and structural heterogeneity observed at the catalytic site suggest that different Ubcs may utilize catalytic mechanisms of varying efficiency and substrate specificity. PubMed: 9261152DOI: 10.1074/jbc.272.34.21381 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
