1YD8

COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN

Summary for 1YD8

• Entry DOI: 10.2210/pdb1yd8/pdb
• Descriptor: UBIQUIN, ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3 (3 entities in total)
• Functional Keywords: trafficking, post translational modification, mono-ubiquitination, protein transport;, protein transport, chromosomal protein
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein : Q9NZ52
• Total number of polymer chains: 4
• Total formula weight: 39584.63

Authors

Prag, G.,Lee, S.,Mattera, R.,Arighi, C.N.,Beach, B.M.,Bonifacino, J.S.,Hurley, J.H. (deposition date: 2004-12-23, release date: 2005-02-22, Last modification date: 2024-04-03)

Primary citation

Prag, G.,Lee, S.,Mattera, R.,Arighi, C.N.,Beach, B.M.,Bonifacino, J.S.,Hurley, J.H.
Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, {gamma}-ear-containing, ADP-ribosylation-factor-binding proteins
Proc.Natl.Acad.Sci.USA, 102:2334-2339, 2005

PubMed Abstract: 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.

PubMed: 15701688
DOI: 10.1073/pnas.0500118102

Experimental method

X-RAY DIFFRACTION (2.8 Å)