1WR6

Crystal structure of GGA3 GAT domain in complex with ubiquitin

Summary for 1WR6

• Entry DOI: 10.2210/pdb1wr6/pdb
• Descriptor: ADP-ribosylation factor binding protein GGA3, ubiquitin (3 entities in total)
• Functional Keywords: three-helix bundle, ubiquitin-binding protein, clathrin coat adaptor protein, protein transport-signaling protein complex, protein transport/signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9NZ52
• Total number of polymer chains: 8
• Total formula weight: 85133.94

Authors

Kawasaki, M.,Shiba, T.,Shiba, Y.,Yamaguchi, Y.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Kato, K.,Nakayama, K.,Wakatsuki, S. (deposition date: 2004-10-12, release date: 2005-06-28, Last modification date: 2024-10-16)

Primary citation

Kawasaki, M.,Shiba, T.,Shiba, Y.,Yamaguchi, Y.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Kato, K.,Nakayama, K.,Wakatsuki, S.
Molecular mechanism of ubiquitin recognition by GGA3 GAT domain.
Genes Cells, 10:639-654, 2005

PubMed Abstract: GGA (Golgi-localizing, gamma-adaptin ear domain homology, ARF-binding) proteins, which constitute a family of clathrin coat adaptor proteins, have recently been shown to be involved in the ubiquitin-dependent sorting of receptors, through the interaction between the C-terminal three-helix-bundle of the GAT (GGA and Tom1) domain (C-GAT) and ubiquitin. We report here the crystal structure of human GGA3 C-GAT in complex with ubiquitin. A hydrophobic patch on C-GAT helices alpha1 and alpha2 forms a binding site for the hydrophobic Ile44 surface of ubiquitin. Two distinct orientations of ubiquitin Arg42 determine the shape and the charge distribution of ubiquitin Ile44 surface, leading to two different binding modes. Biochemical and NMR data strongly suggest another hydrophobic binding site on C-GAT helices alpha2 and alpha3, opposite to the first binding site, also binds ubiquitin although weakly. The double-sided ubiquitin binding provides the GAT domain with higher efficiency in recognizing ubiquitinated receptors for lysosomal receptor degradation.

PubMed: 15966896
DOI: 10.1111/j.1365-2443.2005.00865.x

Experimental method

X-RAY DIFFRACTION (2.6 Å)