3RLE
Crystal Structure of GRASP55 GRASP domain (residues 7-208)
Summary for 3RLE
| Entry DOI | 10.2210/pdb3rle/pdb |
| Descriptor | Golgi reassembly-stacking protein 2 (2 entities in total) |
| Functional Keywords | pdz, tether, golgin, golgi, membrane protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Golgi apparatus membrane; Lipid-anchor: Q9H8Y8 |
| Total number of polymer chains | 1 |
| Total formula weight | 22992.21 |
| Authors | Truschel, S.T.,Sengupta, D.,Foote, A.,Heroux, A.,Macbeth, M.R.,Linstedt, A.D. (deposition date: 2011-04-19, release date: 2011-05-04, Last modification date: 2024-10-09) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.649 Å) |
Structure validation
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