1O3X

Crystal structure of human GGA1 GAT domain

「1J2H」から置き換えられました

1O3X の概要

• エントリーDOI: 10.2210/pdb1o3x/pdb
• 関連するPDBエントリー: 1J2I 1J2J
• 分子名称: ADP-ribosylation factor binding protein GGA1 (2 entities in total)
• 機能のキーワード: protein transport
• 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: 16000.13

構造登録者

Shiba, T.,Kawasaki, M.,Takatsu, H.,Nogi, T.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Nakayama, K.,Wakatsuki, S. (登録日: 2003-05-08, 公開日: 2003-05-20, 最終更新日: 2023-12-27)

主引用文献

Shiba, T.,Kawasaki, M.,Takatsu, H.,Nogi, T.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Nakayama, K.,Wakatsuki, S.
Molecular Mechanism of Membrane Recruitment of Gga by Arf in Lysosomal Protein Transport
Nat.Struct.Biol., 10:386-393, 2003

PubMed Abstract: GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP.

PubMed: 12679809
DOI: 10.1038/nsb920

実験手法

X-RAY DIFFRACTION (2.1 Å)