1VDE
PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY
1VDE の概要
エントリーDOI | 10.2210/pdb1vde/pdb |
分子名称 | PI-SCEI (2 entities in total) |
機能のキーワード | homing endonuclease, protein splicing, endonuclease |
由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
細胞内の位置 | Endomembrane system: P17255 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 102007.79 |
構造登録者 | |
主引用文献 | Duan, X.,Gimble, F.S.,Quiocho, F.A. Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Cell(Cambridge,Mass.), 89:555-564, 1997 Cited by PubMed Abstract: PI-Scel is a bifunctional yeast protein that propagates its mobile gene by catalyzing protein splicing and site-specific DNA double-strand cleavage. Here, we report the 2.4 A crystal structure of the PI-Scel protein. The structure is composed of two separate domains (I and II) with novel folds and different functions. Domain I, which is elongated and formed largely from seven beta sheets, harbors the N and C termini residues and two His residues that are implicated in protein splicing. Domain II, which is compact and is primarily composed of two similar alpha/beta motifs related by local two-fold symmetry, contains the putative nuclease active site with a cluster of two acidic residues and one basic residue commonly found in restriction endonucleases. This report presents prototypic structures of domains with single endonuclease and protein splicing active sites. PubMed: 9160747DOI: 10.1016/S0092-8674(00)80237-8 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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