1OXZ

Crystal Structure of the Human GGA1 GAT domain

1OXZ の概要

• エントリーDOI: 10.2210/pdb1oxz/pdb
• 分子名称: ADP-ribosylation factor binding protein GGA1 (1 entity in total)
• 機能のキーワード: gga1, gat domain, membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9UJY5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20702.45

構造登録者

Zhu, G.,Zhai, P.,He, X.,Terzyan, S.,Zhang, R.,Joachimiak, A.,Tang, J.,Zhang, X.C. (登録日: 2003-04-03, 公開日: 2003-04-15, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)