2j3r
From Proteopedia
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|PDB= 2j3r |SIZE=350|CAPTION= <scene name='initialview01'>2j3r</scene>, resolution 2.6Å | |PDB= 2j3r |SIZE=350|CAPTION= <scene name='initialview01'>2j3r</scene>, resolution 2.6Å | ||
|SITE= <scene name='pdbsite=AC1:No3+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:No3+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=NO3:NITRATE ION'>NO3</scene> | + | |LIGAND= <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=P1L:S-PALMITOYL-L-CYSTEINE'>P1L</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3r OCA], [http://www.ebi.ac.uk/pdbsum/2j3r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j3r RCSB]</span> | ||
}} | }} | ||
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[[Category: Kim, Y G.]] | [[Category: Kim, Y G.]] | ||
[[Category: Oh, B H.]] | [[Category: Oh, B H.]] | ||
| - | [[Category: NO3]] | ||
[[Category: endoplasmic reticulum]] | [[Category: endoplasmic reticulum]] | ||
[[Category: er-golgi transport]] | [[Category: er-golgi transport]] | ||
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[[Category: vesicle transport]] | [[Category: vesicle transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:30 2008'' |
Revision as of 00:52, 31 March 2008
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| , resolution 2.6Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF THE BET3-TRS31 HETERODIMER.
Overview
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.
About this Structure
2J3R is a Protein complex structure of sequences from Danio rerio and Mus musculus. Full crystallographic information is available from OCA.
Reference
The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering., Kim YG, Raunser S, Munger C, Wagner J, Song YL, Cygler M, Walz T, Oh BH, Sacher M, Cell. 2006 Nov 17;127(4):817-30. PMID:17110339
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