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Crystallographic analysis of murine p24γ2 Golgi dynamics domain
Author(s) -
Nagae Masamichi,
Liebschner Dorothee,
Yamada Yusuke,
MoritaMatsumoto Kana,
Matsugaki Naohiro,
Senda Toshiya,
Fujita Morihisa,
Kinoshita Taroh,
Yamaguchi Yoshiki
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25242
Subject(s) - golgi apparatus , dimer , endoplasmic reticulum , crystallography , chemistry , helix (gastropod) , domain (mathematical analysis) , protein domain , biophysics , biochemistry , biology , gene , ecology , mathematical analysis , mathematics , organic chemistry , snail
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.