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| {{STRUCTURE_2j3w| PDB=2j3w | SCENE= }} | | {{STRUCTURE_2j3w| PDB=2j3w | SCENE= }} |
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| '''THE CRYSTAL STRUCTURE OF THE BET3-TRS31-SEDLIN COMPLEX.'''
| | ===THE CRYSTAL STRUCTURE OF THE BET3-TRS31-SEDLIN COMPLEX.=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17110339}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17110339 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17110339}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Trapp]] | | [[Category: Trapp]] |
| [[Category: Vesicle transport]] | | [[Category: Vesicle transport]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:17:47 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:42:41 2008'' |
