Crystallographic analysis of murine p24γ2 Golgi dynamics domain
Crystallographic analysis of murine p24γ2 Golgi dynamics domain
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DOI：
10.1002/prot.25242
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发表时间：
2017-04-01
影响因子：
2.9
通讯作者：
Yamaguchi, Yoshiki
中科院分区：
文献类型：
--
作者：
Nagae, Masamichi;Liebschner, Dorothee;Yamaguchi, Yoshiki
p24家族蛋白形成同源和异源寡聚复合物，用于将货物蛋白从内质网有效转运到高尔基体。它由四个亚家族（p24 alpha，p24 beta，p24 gamma和p24 delta）组成。p24 γ 2在糖基磷脂酰肌醇锚定蛋白的选择性转运中起关键作用。在这里，我们确定了小鼠p242高尔基体动力学（GOLD）域的晶体结构在2.8埃分辨率的单异常衍射方法使用固有的硫原子。尽管p24家族蛋白之间的低序列同一性，但p24 γ 2 GOLD结构域呈现与p24 β 1或p24 δ 1类似的β-夹心折叠。在p24 γ 2 GOLD结构域的C-末端观察到另外的短α-螺旋。有趣的是，p24 γ 2 GOLD结构域结晶为二聚体，并且二聚体的形成似乎由短α-螺旋辅助。在p24家族蛋白中比较GOLD结构域的二聚化模式。(C)2016 Wiley Periodicals，Inc.
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 (p24 alpha, p24 beta, p24 gamma, and p24 delta). p24 gamma 2 plays crucial roles in the selective transport of glycosylphosphatidylinositol-anchored proteins. Here, we determined the crystal structure of mouse p242 Golgi dynamics (GOLD) domain at 2.8 angstrom resolution by the single anomalous diffraction method using intrinsic sulfur atoms. In spite of low sequence identity among p24 family proteins, p24 gamma 2 GOLD domain assumes beta-sandwich fold, similar to that of p24 beta 1 or p24 delta 1. An additional short alpha-helix is observed at the C-terminus of the p24 gamma 2 GOLD domain. Intriguingly, p24 gamma 2 GOLD domains crystallize as dimers, and dimer formation seems assisted by the short alpha-helix. Dimerization modes of GOLD domains are compared among p24 family proteins. (C) 2016 Wiley Periodicals, Inc.