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2j3r

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==Overview==
==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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?17110339 (full description)]]
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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.
==About this Structure==
==About this Structure==
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2J3R is a [[http://en.wikipedia.org/wiki/Protein_complex 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]] with NO3 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J3R OCA]].
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2J3R is a [http://en.wikipedia.org/wiki/Protein_complex 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] with NO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J3R OCA].
==Reference==
==Reference==
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[[Category: vesicle transport]]
[[Category: vesicle transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:23:32 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:07:25 2007''

Revision as of 12:02, 5 November 2007


2j3r, resolution 2.6Å

Drag the structure with the mouse to rotate

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 with NO3 as ligand. Structure known Active Site: AC1. 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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