1X79

Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5

Summary for 1X79

• Entry DOI: 10.2210/pdb1x79/pdb
• Descriptor: ADP-ribosylation factor binding protein GGA1, Rab GTPase binding effector protein 1, SULFATE ION, ... (5 entities in total)
• Functional Keywords: rabaptin5, gga protein, gat domain, intracellular trafficking, protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9UJY5; Cytoplasm: Q15276
• Total number of polymer chains: 3
• Total formula weight: 37261.98

Authors

Zhu, G.,Zhang, X.C. (deposition date: 2004-08-13, release date: 2004-10-12, Last modification date: 2024-02-14)

Primary citation

Zhu, G.,Zhai, P.,He, X.,Wakeham, N.,Rodgers, K.,Li, G.,Tang, J.,Zhang, X.C.
Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5.
EMBO J., 23:3909-3917, 2004

PubMed Abstract: GGA proteins coordinate the intracellular trafficking of clathrin-coated vesicles through their interaction with several other proteins. The GAT domain of GGA proteins interacts with ARF, ubiquitin, and Rabaptin5. The GGA-Rabaptin5 interaction is believed to function in the fusion of trans-Golgi-derived vesicles to endosomes. We determined the crystal structure of a human GGA1 GAT domain fragment in complex with the Rabaptin5 GAT-binding domain. In this structure, the Rabaptin5 domain is a 90-residue-long helix. At the N-terminal end, it forms a parallel coiled-coil homodimer, which binds one GAT domain of GGA1. In the C-terminal region, it further assembles into a four-helix bundle tetramer. The Rabaptin5-binding motif of the GGA1 GAT domain consists of a three-helix bundle. Thus, the binding between Rabaptin5 and GGA1 GAT domain is based on a helix bundle-helix bundle interaction. The current structural observation is consistent with previously reported mutagenesis data, and its biological relevance is further confirmed by new mutagenesis studies and affinity analysis. The four-helix bundle structure of Rabaptin5 suggests a functional role in tethering organelles.

PubMed: 15457209
DOI: 10.1038/sj.emboj.7600411

Experimental method

X-RAY DIFFRACTION (2.41 Å)