2j3w

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(New page: 200px<br /><applet load="2j3w" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j3w, resolution 2.1&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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'''THE CRYSTAL STRUCTURE OF THE BET3-TRS31-SEDLIN COMPLEX.'''<br />
'''THE CRYSTAL STRUCTURE OF THE BET3-TRS31-SEDLIN COMPLEX.'''<br />
==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, 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.
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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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2J3W 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]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J3W OCA].
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2J3W 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3W OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Kim, Y.G.]]
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[[Category: Kim, Y G.]]
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[[Category: Oh, B.H.]]
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[[Category: Oh, B H.]]
[[Category: endoplasmic reticulum]]
[[Category: endoplasmic reticulum]]
[[Category: er-golgi transport]]
[[Category: er-golgi transport]]
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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 Wed Nov 21 12:32:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:56 2008''

Revision as of 15:58, 21 February 2008


2j3w, resolution 2.1Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE OF THE BET3-TRS31-SEDLIN COMPLEX.

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

2J3W 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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