1yd8: Difference between revisions
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[[Image:1yd8.gif|left|200px]] | [[Image:1yd8.gif|left|200px]] | ||
'''COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN''' | {{Structure | ||
|PDB= 1yd8 |SIZE=350|CAPTION= <scene name='initialview01'>1yd8</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= GGA3, KIAA0154 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1YD8 is a [ | 1YD8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD8 OCA]. | ||
==Reference== | ==Reference== | ||
Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins., Prag G, Lee S, Mattera R, Arighi CN, Beach BM, Bonifacino JS, Hurley JH, Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2334-9. Epub 2005 Feb 8. PMID:[http:// | Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins., Prag G, Lee S, Mattera R, Arighi CN, Beach BM, Bonifacino JS, Hurley JH, Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2334-9. Epub 2005 Feb 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15701688 15701688] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: trafficking]] | [[Category: trafficking]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:21:21 2008'' | ||
Revision as of 16:21, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Gene: | GGA3, KIAA0154 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
OverviewOverview
The Golgi-localized, gamma-ear-containing, Arf (ADP-ribosylation factor)-binding (GGA) proteins are clathrin adaptors that mediate the sorting of transmembrane-cargo molecules at the trans-Golgi network and endosomes. Cargo proteins can be directed into the GGA pathway by at least two different types of sorting signals: acidic cluster-dileucine motifs and covalent modification by ubiquitin. The latter modification is recognized by the GGAs through binding to their GAT [GGA and TOM (target of Myb)] domain. Here we report the crystal structure of the GAT domain of human GGA3 in a 1:1 complex with ubiquitin at 2.8-A resolution. Ubiquitin binds to a hydrophobic and acidic patch on helices alpha1 and alpha2 of the GAT three-helix bundle that includes Asn-223, Leu-227, Glu-230, Met-231, Asp-244, Glu-246, Leu-247, Glu-250, and Leu-251. The GAT-binding surface on ubiquitin is a hydrophobic patch centered on Ile-44 that is also responsible for binding most other ubiquitin effectors. The ubiquitin-binding site observed in the crystal is distinct from the Rabaptin-5-binding site on helices alpha2 and alpha3 of the GAT domain. Mutational analysis and modeling of the ubiquitin-Rabaptin-5-GAT ternary complex indicates that ubiquitin and Rabaptin-5 can bind to the GAT domain at two different sites without any steric conflict. This ability highlights the GAT domain as a hub for interactions with multiple partners in trafficking.
About this StructureAbout this Structure
1YD8 is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins., Prag G, Lee S, Mattera R, Arighi CN, Beach BM, Bonifacino JS, Hurley JH, Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2334-9. Epub 2005 Feb 8. PMID:15701688
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