1OXZ

Crystal Structure of the Human GGA1 GAT domain

Summary for 1OXZ

• Entry DOI: 10.2210/pdb1oxz/pdb
• Descriptor: ADP-ribosylation factor binding protein GGA1 (1 entity in total)
• Functional Keywords: gga1, gat domain, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9UJY5
• Total number of polymer chains: 1
• Total formula weight: 20702.45

Authors

Zhu, G.,Zhai, P.,He, X.,Terzyan, S.,Zhang, R.,Joachimiak, A.,Tang, J.,Zhang, X.C. (deposition date: 2003-04-03, release date: 2003-04-15, Last modification date: 2024-02-14)

Primary citation

Zhu, G.,Zhai, P.,He, X.,Terzyan, S.,Zhang, R.,Joachimiak, A.,Tang, J.,Zhang, X.C.
Crystal Structure of Human GGA1 GAT Domain
Biochemistry, 42:6392-6399, 2003

PubMed Abstract: GGAs are a family of vesicle-coating regulatory proteins that function in intracellular protein transport. A GGA molecule contains four domains, each mediating interaction with other proteins in carrying out intracellular transport. The GAT domain of GGAs has been identified as the structural entity that binds membrane-bound ARF, a molecular switch regulating vesicle-coat assembly. It also directly interacts with rabaptin5, an essential component of endosome fusion. A 2.8 A resolution crystal structure of the human GGA1 GAT domain is reported here. The GAT domain contains four helices and has an elongated shape with the longest dimension exceeding 80 A. Its longest helix is involved in two structural motifs: an N-terminal helix-loop-helix motif and a C-terminal three-helix bundle. The N-terminal motif harbors the most conservative amino acid sequence in the GGA GAT domains. Within this conserved region, a cluster of residues previously implicated in ARF binding forms a hydrophobic surface patch, which is likely to be the ARF-binding site. In addition, a structure-based mutagenesis-biochemical analysis demonstrates that the C-terminal three-helix bundle of this GAT domain is responsible for the rabaptin5 binding. These structural characteristics are consistent with a model supporting multiple functional roles for the GAT domain.

PubMed: 12767220
DOI: 10.1021/bi034334n

Experimental method

X-RAY DIFFRACTION (2.8 Å)