2j3r: Difference between revisions
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[[Image:2j3r.jpg|left|200px]] | [[Image:2j3r.jpg|left|200px]] | ||
'''THE CRYSTAL STRUCTURE OF THE BET3-TRS31 HETERODIMER.''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=NO3:NITRATE ION'>NO3</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF THE BET3-TRS31 HETERODIMER.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2J3R is a [ | 2J3R is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3R OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17110339 17110339] | ||
[[Category: Danio rerio]] | [[Category: Danio rerio]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: vesicle transport]] | [[Category: vesicle transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:36:51 2008'' | ||
Revision as of 15:36, 20 March 2008
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| 2j3r, resolution 2.6Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | NO3 | ||||||||||||
| 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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