1yd8

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{{STRUCTURE_1yd8| PDB=1yd8 | SCENE= }}
{{STRUCTURE_1yd8| PDB=1yd8 | SCENE= }}
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'''COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN'''
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===COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15701688}}
==About this Structure==
==About this Structure==
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[[Category: Protein transport;]]
[[Category: Protein transport;]]
[[Category: Trafficking]]
[[Category: Trafficking]]
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Revision as of 18:03, 27 July 2008

Image:1yd8.png

Template:STRUCTURE 1yd8

COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN

Template:ABSTRACT PUBMED 15701688

About this Structure

1YD8 is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.

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:15701688

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