2j3r
From Proteopedia
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[[Category: vesicle transport]] | [[Category: vesicle transport]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:23:32 2007'' |
Revision as of 15:18, 30 October 2007
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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, ... [(full description)]
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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