1A3S
HUMAN UBC9
1A3S の概要
エントリーDOI | 10.2210/pdb1a3s/pdb |
分子名称 | UBC9 (1 entity in total) |
機能のキーワード | sumo conjugating enzyme, ubiquitin conjugating enzyme |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Nucleus: P63279 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 18174.94 |
構造登録者 | |
主引用文献 | Giraud, M.F.,Desterro, J.M.,Naismith, J.H. Structure of ubiquitin-conjugating enzyme 9 displays significant differences with other ubiquitin-conjugating enzymes which may reflect its specificity for sumo rather than ubiquitin. Acta Crystallogr.,Sect.D, 54:891-898, 1998 Cited by PubMed Abstract: The three-dimensional structure of ubiquitin-conjugating enzyme 9 (Ubc9) has been obtained to a resolution of 2.8 A by molecular replacement followed by a combination of automated refinement and graphical intervention. Diffraction data were recorded on a single crystal in space group P43 with cell dimensions a = b = 73.9, c = 42. 9 A. The final model has an R factor of 21.3% for all data to 2.8 A. Only the N-terminal methionine, a two-residue N-terminal extension and a four-residue loop are not located by the final electron-density map. Ubc9 is now known to be the first sumo, a new ubiquitin-like protein, conjugating enzyme and does not conjugate ubiquitin. The structure of Ubc9 shows important differences compared with the structures of known ubiquitin-conjugating enzymes. At the N-terminal helix, the structural and sequence alignments are out of register by one amino acid giving Ubc9 a different recognition surface compared to ubiquitin-conjugating enzymes. This is coupled to a profound change in the electrostatic surface of the molecular face remote from the catalytic site. These differences may be important in recognition of other proteins in the Sumo conjugation pathway. The catalytic cysteine in Ubc9 has a positively charged lip and a negatively charged ridge nearby. Both these features seem confined to sumo-conjugating enzymes, and a sequence alignment of sumo and ubiquitin suggests how these might play a role in sumo/ubiquitin discrimination. PubMed: 9757105DOI: 10.1107/S0907444998002480 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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