5GU5

Crystal structure of p24gamma2 GOLD domain determined by sulfur-SAD

5GU5 の概要

• エントリーDOI: 10.2210/pdb5gu5/pdb
• 分子名称: Transmembrane emp24 domain-containing protein 5, BROMIDE ION (2 entities in total)
• 機能のキーワード: transport protein, gpi-anchored protein, p24 protein family
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13294.33

構造登録者

Nagae, M.,Yamaguchi, Y. (登録日: 2016-08-25, 公開日: 2017-01-25, 最終更新日: 2024-11-13)

主引用文献

Nagae, M.,Liebschner, D.,Yamada, Y.,Morita-Matsumoto, K.,Matsugaki, N.,Senda, T.,Fujita, M.,Kinoshita, T.,Yamaguchi, Y.
Crystallographic analysis of murine p24 gamma 2 Golgi dynamics domain
Proteins, 85:764-770, 2017

PubMed Abstract: The p24 family proteins form homo- and hetero-oligomeric complexes for efficient transport of cargo proteins from the endoplasmic reticulum to the Golgi apparatus. It consists of four subfamilies (p24α, p24β, p24γ, and p24δ). p24γ2 plays crucial roles in the selective transport of glycosylphosphatidylinositol-anchored proteins. Here, we determined the crystal structure of mouse p24γ2 Golgi dynamics (GOLD) domain at 2.8 Å resolution by the single anomalous diffraction method using intrinsic sulfur atoms. In spite of low sequence identity among p24 family proteins, p24γ2 GOLD domain assumes a β-sandwich fold, similar to that of p24β1 or p24δ1. An additional short α-helix is observed at the C-terminus of the p24γ2 GOLD domain. Intriguingly, p24γ2 GOLD domains crystallize as dimers, and dimer formation seems assisted by the short α-helix. Dimerization modes of GOLD domains are compared among p24 family proteins. Proteins 2017; 85:764-770. © 2016 Wiley Periodicals, Inc.

PubMed: 28066915
DOI: 10.1002/prot.25242

実験手法

X-RAY DIFFRACTION (2.8 Å)