1C7R
THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE/AUTOCRINE MOTILITY FACTOR/NEUROLEUKIN COMPLEXED WITH ITS CARBOHYDRATE PHOSPHATE INHIBITORS AND ITS SUBSTRATE RECOGNITION MECHANISM
1C7R の概要
| エントリーDOI | 10.2210/pdb1c7r/pdb |
| 関連するPDBエントリー | 1C7Q |
| 分子名称 | PHOSPHOGLUCOSE ISOMERASE, 5-PHOSPHOARABINONIC ACID (3 entities in total) |
| 機能のキーワード | phosphoglucose isomerase/autocrine motility factor/ neuroleukin, isomerase |
| 由来する生物種 | Geobacillus stearothermophilus |
| 細胞内の位置 | Cytoplasm: P13376 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 50448.87 |
| 構造登録者 | |
| 主引用文献 | Chou, C.C.,Sun, Y.J.,Meng, M.,Hsiao, C.D. The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition. J.Biol.Chem., 275:23154-23160, 2000 Cited by PubMed Abstract: Phosphoglucose isomerase catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-A resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His(306)) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase. PubMed: 10770936DOI: 10.1074/jbc.M002017200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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