3RLE
Crystal Structure of GRASP55 GRASP domain (residues 7-208)
3RLE の概要
| エントリーDOI | 10.2210/pdb3rle/pdb |
| 分子名称 | Golgi reassembly-stacking protein 2 (2 entities in total) |
| 機能のキーワード | pdz, tether, golgin, golgi, membrane protein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Golgi apparatus membrane; Lipid-anchor: Q9H8Y8 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 22992.21 |
| 構造登録者 | Truschel, S.T.,Sengupta, D.,Foote, A.,Heroux, A.,Macbeth, M.R.,Linstedt, A.D. (登録日: 2011-04-19, 公開日: 2011-05-04, 最終更新日: 2024-10-09) |
| 主引用文献 | Truschel, S.T.,Sengupta, D.,Foote, A.,Heroux, A.,Macbeth, M.R.,Linstedt, A.D. Structure of the Membrane-tethering GRASP Domain Reveals a Unique PDZ Ligand Interaction That Mediates Golgi Biogenesis. J.Biol.Chem., 286:20125-20129, 2011 Cited by PubMed Abstract: Biogenesis of the ribbon-like membrane network of the mammalian Golgi requires membrane tethering by the conserved GRASP domain in GRASP65 and GRASP55, yet the tethering mechanism is not fully understood. Here, we report the crystal structure of the GRASP55 GRASP domain, which revealed an unusual arrangement of two tandem PDZ folds that more closely resemble prokaryotic PDZ domains. Biochemical and functional data indicated that the interaction between the ligand-binding pocket of PDZ1 and an internal ligand on PDZ2 mediates the GRASP self-interaction, and structural analyses suggest that this occurs via a unique mode of internal PDZ ligand recognition. Our data uncover the structural basis for ligand specificity and provide insight into the mechanism of GRASP-dependent membrane tethering of analogous Golgi cisternae. PubMed: 21515684DOI: 10.1074/jbc.C111.245324 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.649 Å) |
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