5Z39

Crystal structure of C terminal region of G-protein interacting protein 1 (Gip1) from Dictyostelium discoideum form II

5Z39 の概要

• エントリーDOI: 10.2210/pdb5z39/pdb
• 分子名称: G-protein interacting protein 1, DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE, ... (5 entities in total)
• 機能のキーワード: alpha helix, lipid binding, g-protein binding, social amoebae, chemotaxis, protein binding
• 由来する生物種: Dictyostelium discoideum (Slime mold)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20756.40

構造登録者

Miyagawa, T.,Koteishi, H.,Kamimura, Y.,Miyanaga, Y.,Takeshita, K.,Nakagawa, A.,Ueda, M. (登録日: 2018-01-05, 公開日: 2018-10-17, 最終更新日: 2023-11-22)

主引用文献

Miyagawa, T.,Koteishi, H.,Kamimura, Y.,Miyanaga, Y.,Takeshita, K.,Nakagawa, A.,Ueda, M.
Structural basis of Gip1 for cytosolic sequestration of G protein in wide-range chemotaxis
Nat Commun, 9:4635-4635, 2018

PubMed Abstract: G protein interacting protein 1 (Gip1) binds and sequesters heterotrimeric G proteins in the cytosolic pool, thus regulating G protein-coupled receptor (GPCR) signalling for eukaryotic chemotaxis. Here, we report the underlying structural basis of Gip1 function. The crystal structure reveals that the region of Gip1 that binds to the G protein has a cylinder-like fold with a central hydrophobic cavity composed of six α-helices. Mutagenesis and biochemical analyses indicate that the hydrophobic cavity and the hydrogen bond network at the entrance of the cavity are essential for complex formation with the geranylgeranyl modification on the Gγ subunit. Mutations of the cavity impair G protein sequestration and translocation to the membrane from the cytosol upon receptor stimulation, leading to defects in chemotaxis at higher chemoattractant concentrations. These results demonstrate that the Gip1-dependent regulation of G protein shuttling ensures wide-range gradient sensing in eukaryotic chemotaxis.

PubMed: 30401901
DOI: 10.1038/s41467-018-07035-x

実験手法

X-RAY DIFFRACTION (2.74 Å)