2J3W
The crystal structure of the bet3-trs31-sedlin complex.
Summary for 2J3W
| Entry DOI | 10.2210/pdb2j3w/pdb |
| Related | 2J3R 2J3T |
| Descriptor | TRAFFICKING PROTEIN PARTICLE COMPLEX PROTEIN 2, ZGC 92866, TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3, ... (5 entities in total) |
| Functional Keywords | multisubunit tethering factor, trapp, palmitate, transport, lipoprotein, er-golgi transport, endoplasmic reticulum, transcription, golgi apparatus, vesicle transport |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Cellular location | Golgi apparatus (By similarity): Q9CQP2 Golgi apparatus, cis-Golgi network (By similarity): 2J3W |
| Total number of polymer chains | 6 |
| Total formula weight | 116946.09 |
| Authors | Kim, Y.-G.,Oh, B.-H. (deposition date: 2006-08-23, release date: 2006-11-27, Last modification date: 2024-10-23) |
| Primary citation | Kim, Y.-G.,Raunser, S.,Munger, C.,Wagner, J.,Song, Y.-L.,Cygler, M.,Walz, T.,Oh, B.-H.,Sacher, M. The Architecture of the Multisubunit Trapp I Complex Suggests a Model for Vesicle Tethering. Cell(Cambridge,Mass.), 127:817-, 2006 Cited by PubMed Abstract: Transport protein particle (TRAPP) I is a multisubunit vesicle tethering factor composed of seven subunits involved in ER-to-Golgi trafficking. The functional mechanism of the complex and how the subunits interact to form a functional unit are unknown. Here, we have used a multidisciplinary approach that includes X-ray crystallography, electron microscopy, biochemistry, and yeast genetics to elucidate the architecture of TRAPP I. The complex is organized through lateral juxtaposition of the subunits into a flat and elongated particle. We have also localized the site of guanine nucleotide exchange activity to a highly conserved surface encompassing several subunits. We propose that TRAPP I attaches to Golgi membranes with its large flat surface containing many highly conserved residues and forms a platform for protein-protein interactions. This study provides the most comprehensive view of a multisubunit vesicle tethering complex to date, based on which a model for the function of this complex, involving Rab1-GTP and long, coiled-coil tethers, is presented. PubMed: 17110339DOI: 10.1016/J.CELL.2006.09.029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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