1yd8
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(New page: 200px<br /> <applet load="1yd8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yd8, resolution 2.80Å" /> '''COMPLEX OF HUMAN GG...)
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Revision as of 18:11, 12 November 2007
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COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
Overview
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 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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