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2J3R

The crystal structure of the bet3-trs31 heterodimer.

Summary for 2J3R
Entry DOI10.2210/pdb2j3r/pdb
Related1VPG 1WC8 1WC9 2J3T 2J3W
DescriptorTRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3, ZGC 92866, PALMITIC ACID, ... (5 entities in total)
Functional Keywordsgolgi apparatus, vesicle transport, er-golgi transport, trapp, palmitate, transport, lipoprotein, endoplasmic reticulum, multisubunit tethering factor
Biological sourceMUS MUSCULUS (MOUSE)
More
Cellular locationGolgi apparatus, cis-Golgi network (By similarity): O55013
Total number of polymer chains2
Total formula weight38306.89
Authors
Kim, Y.-G.,Oh, B.-H. (deposition date: 2006-08-23, release date: 2006-11-27, Last modification date: 2011-10-26)
Primary citationKim, 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: 17110339
DOI: 10.1016/J.CELL.2006.09.029
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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