1wr6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1wr6.gif|left|200px]] | [[Image:1wr6.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1wr6", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1wr6| PDB=1wr6 | SCENE= }} | |||
}} | |||
'''Crystal structure of GGA3 GAT domain in complex with ubiquitin''' | '''Crystal structure of GGA3 GAT domain in complex with ubiquitin''' | ||
| Line 37: | Line 34: | ||
[[Category: Wakatsuki, S.]] | [[Category: Wakatsuki, S.]] | ||
[[Category: Yamaguchi, Y.]] | [[Category: Yamaguchi, Y.]] | ||
[[Category: | [[Category: Clathrin coat adaptor protein]] | ||
[[Category: | [[Category: Three-helix bundle]] | ||
[[Category: | [[Category: Ubiquitin-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:02:31 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 14:02, 3 May 2008
Crystal structure of GGA3 GAT domain in complex with ubiquitin
OverviewOverview
GGA (Golgi-localizing, gamma-adaptin ear domain homology, ARF-binding) proteins, which constitute a family of clathrin coat adaptor proteins, have recently been shown to be involved in the ubiquitin-dependent sorting of receptors, through the interaction between the C-terminal three-helix-bundle of the GAT (GGA and Tom1) domain (C-GAT) and ubiquitin. We report here the crystal structure of human GGA3 C-GAT in complex with ubiquitin. A hydrophobic patch on C-GAT helices alpha1 and alpha2 forms a binding site for the hydrophobic Ile44 surface of ubiquitin. Two distinct orientations of ubiquitin Arg42 determine the shape and the charge distribution of ubiquitin Ile44 surface, leading to two different binding modes. Biochemical and NMR data strongly suggest another hydrophobic binding site on C-GAT helices alpha2 and alpha3, opposite to the first binding site, also binds ubiquitin although weakly. The double-sided ubiquitin binding provides the GAT domain with higher efficiency in recognizing ubiquitinated receptors for lysosomal receptor degradation.
About this StructureAbout this Structure
1WR6 is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Molecular mechanism of ubiquitin recognition by GGA3 GAT domain., Kawasaki M, Shiba T, Shiba Y, Yamaguchi Y, Matsugaki N, Igarashi N, Suzuki M, Kato R, Kato K, Nakayama K, Wakatsuki S, Genes Cells. 2005 Jul;10(7):639-54. PMID:15966896 Page seeded by OCA on Sat May 3 14:02:31 2008