1x79
From Proteopedia
(New page: 200px<br /> <applet load="1x79" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x79, resolution 2.41Å" /> '''Crystal structure o...) |
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| - | [[Image:1x79.gif|left|200px]]<br /> | + | [[Image:1x79.gif|left|200px]]<br /><applet load="1x79" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1x79, resolution 2.41Å" /> | caption="1x79, resolution 2.41Å" /> | ||
'''Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5'''<br /> | '''Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | GGA proteins coordinate the intracellular trafficking of clathrin-coated | + | GGA proteins coordinate the intracellular trafficking of clathrin-coated vesicles through their interaction with several other proteins. The GAT domain of GGA proteins interacts with ARF, ubiquitin, and Rabaptin5. The GGA-Rabaptin5 interaction is believed to function in the fusion of trans-Golgi-derived vesicles to endosomes. We determined the crystal structure of a human GGA1 GAT domain fragment in complex with the Rabaptin5 GAT-binding domain. In this structure, the Rabaptin5 domain is a 90-residue-long helix. At the N-terminal end, it forms a parallel coiled-coil homodimer, which binds one GAT domain of GGA1. In the C-terminal region, it further assembles into a four-helix bundle tetramer. The Rabaptin5-binding motif of the GGA1 GAT domain consists of a three-helix bundle. Thus, the binding between Rabaptin5 and GGA1 GAT domain is based on a helix bundle-helix bundle interaction. The current structural observation is consistent with previously reported mutagenesis data, and its biological relevance is further confirmed by new mutagenesis studies and affinity analysis. The four-helix bundle structure of Rabaptin5 suggests a functional role in tethering organelles. |
==About this Structure== | ==About this Structure== | ||
| - | 1X79 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and DTT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1X79 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=DTT:'>DTT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X79 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Zhang, X | + | [[Category: Zhang, X C.]] |
[[Category: Zhu, G.]] | [[Category: Zhu, G.]] | ||
[[Category: DTT]] | [[Category: DTT]] | ||
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[[Category: rabaptin5]] | [[Category: rabaptin5]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:51:52 2008'' |
Revision as of 13:52, 21 February 2008
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Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5
Overview
GGA proteins coordinate the intracellular trafficking of clathrin-coated vesicles through their interaction with several other proteins. The GAT domain of GGA proteins interacts with ARF, ubiquitin, and Rabaptin5. The GGA-Rabaptin5 interaction is believed to function in the fusion of trans-Golgi-derived vesicles to endosomes. We determined the crystal structure of a human GGA1 GAT domain fragment in complex with the Rabaptin5 GAT-binding domain. In this structure, the Rabaptin5 domain is a 90-residue-long helix. At the N-terminal end, it forms a parallel coiled-coil homodimer, which binds one GAT domain of GGA1. In the C-terminal region, it further assembles into a four-helix bundle tetramer. The Rabaptin5-binding motif of the GGA1 GAT domain consists of a three-helix bundle. Thus, the binding between Rabaptin5 and GGA1 GAT domain is based on a helix bundle-helix bundle interaction. The current structural observation is consistent with previously reported mutagenesis data, and its biological relevance is further confirmed by new mutagenesis studies and affinity analysis. The four-helix bundle structure of Rabaptin5 suggests a functional role in tethering organelles.
About this Structure
1X79 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5., Zhu G, Zhai P, He X, Wakeham N, Rodgers K, Li G, Tang J, Zhang XC, EMBO J. 2004 Oct 13;23(20):3909-17. Epub 2004 Sep 30. PMID:15457209
Page seeded by OCA on Thu Feb 21 15:51:52 2008
Categories: Homo sapiens | Protein complex | Zhang, X C. | Zhu, G. | DTT | SO4 | Gat domain | Gga protein | Intracellular trafficking | Rabaptin5
