2j3r: Difference between revisions

Line 4:

==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.

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==

Line 14:

[[Category: Mus musculus]]

[[Category: Protein complex]]

[[Category: Kim, Y.G.]]

[[Category: Kim, Y G.]]

[[Category: Oh, B.H.]]

[[Category: Oh, B H.]]

[[Category: NO3]]

[[Category: endoplasmic reticulum]]

Line 27:

[[Category: vesicle transport]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:41:14 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:53 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Kim, Y.G.]]
+[[Category: Kim, Y G.]]
-[[Category: Oh, B.H.]]
+[[Category: Oh, B H.]]
 [[Category: NO3]]
 [[Category: endoplasmic reticulum]]
@@ Line 27: / Line 27: @@
 [[Category: vesicle transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:41:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:53 2008''