2J3T

The crystal structure of the bet3-trs33-bet5-trs23 complex.

Summary for 2J3T

• Entry DOI: 10.2210/pdb2j3t/pdb
• Related: 1VPG 1WC8 1WC9 2C0J 2J3R 2J3W
• Descriptor: TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3, TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 6A, TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 1, ... (6 entities in total)
• Functional Keywords: trapp, palmitate, transport, lipoprotein, er-golgi transport, golgi apparatus, protein transport, vesicle transport, endoplasmic reticulum, multisubunit tethering factor
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Golgi apparatus, cis-Golgi network (By similarity): O55013 O75865 Q5NCF2 Q9Y296
• Total number of polymer chains: 4
• Total formula weight: 79600.71

Authors

Kim, Y.,Oh, B. (deposition date: 2006-08-23, release date: 2006-11-22, Last modification date: 2024-10-16)

Primary citation

Kim, Y.,Raunser, S.,Munger, C.,Wagner, J.,Song, Y.,Cygler, M.,Walz, T.,Oh, B.,Sacher, M.
The Architecture of the Multisubunit Trapp I Complex Suggests a Model for Vesicle Tethering.
Cell(Cambridge,Mass.), 127:817-, 2006

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: 17110339
DOI: 10.1016/J.CELL.2006.09.029

Experimental method

X-RAY DIFFRACTION (2.4 Å)