2WSI
Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD
2WSI の概要
| エントリーDOI | 10.2210/pdb2wsi/pdb |
| 分子名称 | FAD SYNTHETASE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| 機能のキーワード | transferase, nucleotidyltransferase, nucleotide-binding |
| 由来する生物種 | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| 細胞内の位置 | Cytoplasm: P38913 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 36462.64 |
| 構造登録者 | |
| 主引用文献 | Leulliot, N.,Blondeau, K.,Keller, J.,Ulryck, N.,Quevillon-Cheruel, S.,Van Tilbeurgh, H. Crystal Structure of Yeast Fad Synthetase (Fad1) in Complex with Fad. J.Mol.Biol., 398:641-, 2010 Cited by PubMed Abstract: Flavin adenine dinucleotide (FAD) synthetase is an essential enzyme responsible for the synthesis of FAD by adenylation of riboflavin monophosphate (FMN). We have solved the 1.9 A resolution structure of Fad1, the yeast FAD synthetase, in complex with the FAD product in the active site. The structure of Fad1 shows it to be a member of the PP-ATPase superfamily. Important conformational differences in the two motifs involved in binding the phosphate moieties of FAD compared to the Candida glabrata FMNT ortholog suggests that this loop is dynamic and undergoes substantial conformational changes during its catalytic cycle. PubMed: 20359485DOI: 10.1016/J.JMB.2010.03.040 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






