5gu5
From Proteopedia
Crystal structure of p24gamma2 GOLD domain determined by sulfur-SAD
Structural highlights
FunctionTMED5_MOUSE Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Required for the maintenance of the Golgi apparatus; involved in protein exchange between Golgi stacks during assembly. Probably not required for COPI-vesicle-mediated retrograde transport (By similarity). Publication Abstract from PubMedThe 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 (p24alpha, p24beta, p24gamma, and p24delta). p24gamma2 plays crucial roles in the selective transport of glycosylphosphatidylinositol-anchored proteins. Here, we determined the crystal structure of mouse p24gamma2 Golgi dynamics (GOLD) domain at 2.8 A resolution by the single anomalous diffraction method using intrinsic sulfur atoms. In spite of low sequence identity among p24 family proteins, p24gamma2 GOLD domain assumes a beta-sandwich fold, similar to that of p24beta1 or p24delta1. An additional short alpha-helix is observed at the C-terminus of the p24gamma2 GOLD domain. Intriguingly, p24gamma2 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. Proteins 2017. (c) 2017 Wiley Periodicals, Inc. Crystallographic analysis of murine p24gamma2 Golgi dynamics domain.,Nagae M, Liebschner D, Yamada Y, Morita-Matsumoto K, Matsugaki N, Senda T, Fujita M, Kinoshita T, Yamaguchi Y Proteins. 2017 Jan 9. doi: 10.1002/prot.25242. PMID:28066915[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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