1EUV
X-RAY STRUCTURE OF THE C-TERMINAL ULP1 PROTEASE DOMAIN IN COMPLEX WITH SMT3, THE YEAST ORTHOLOG OF SUMO.
1EUV の概要
| エントリーDOI | 10.2210/pdb1euv/pdb |
| 分子名称 | ULP1 PROTEASE, UBITQUTIN-LIKE PROTEIN SMT3 (3 entities in total) |
| 機能のキーワード | sumo hydrolase, ubiquitin-like protease 1, smt3 hydrolase desumoylating enzyme, cysteine protease, sumo processing enzyme, smt3 processing enzyme, nabh4, thiohemiacetal, covalent protease adduct, hydrolase |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 35611.58 |
| 構造登録者 | |
| 主引用文献 | Mossessova, E.,Lima, C.D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol.Cell, 5:865-876, 2000 Cited by PubMed Abstract: Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear processes and cell cycle progression in yeast. The Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1) processing of full-length SUMO to its mature form and (2) deconjugation of SUMO from targeted proteins. Selective reduction of the proteolytic reaction produced a covalent thiohemiacetal transition state complex between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing of elements within the conserved interface elucidate determinants of SUMO recognition, processing, and deconjugation. Genetic analysis guided by the structure further reveals a regulatory element N-terminal to the proteolytic domain that is required for cell growth in yeast. PubMed: 10882122DOI: 10.1016/S1097-2765(00)80326-3 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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