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 2.1Å" /> '''THE CRYSTAL STRUCTURE...)
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Revision as of 10:24, 21 November 2007
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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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