5GU5
Crystal structure of p24gamma2 GOLD domain determined by sulfur-SAD
Summary for 5GU5
| Entry DOI | 10.2210/pdb5gu5/pdb |
| Descriptor | Transmembrane emp24 domain-containing protein 5, BROMIDE ION (2 entities in total) |
| Functional Keywords | transport protein, gpi-anchored protein, p24 protein family |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 13294.33 |
| Authors | Nagae, M.,Yamaguchi, Y. (deposition date: 2016-08-25, release date: 2017-01-25, Last modification date: 2024-11-13) |
| Primary citation | 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 Cited by 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: 28066915DOI: 10.1002/prot.25242 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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