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Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution.

Lahav A, Rozenberg H, Parnis A, Cassel D, Adir N
Acta Crystallogr D Biol Crystallogr 71 1328-34 (2015)
Cited: 6 times
EuropePMC logo PMID: 26057672

Abstract

The heptameric COPI coat (coatomer) plays an essential role in vesicular transport in the early secretory system of eukaryotic cells. While the structures of some of the subunits have been determined, that of the δ-COP subunit has not been reported to date. The δ-COP subunit is part of a subcomplex with structural similarity to tetrameric clathrin adaptors (APs), where δ-COP is the structural homologue of the AP μ subunit. Here, the crystal structure of the μ homology domain (MHD) of δ-COP (δ-MHD) obtained by phasing using a combined SAD-MR method is presented at 2.15 Å resolution. The crystallographic asymmetric unit contains two monomers that exhibit short sections of disorder, which may allude to flexible regions of the protein. The δ-MHD is composed of two subdomains connected by unstructured linkers. Comparison between this structure and those of known MHD domains from the APs shows significant differences in the positions of specific loops and β-sheets, as well as a more general change in the relative positions of the protein subdomains. The identified difference may be the major source of cargo-binding specificity. Finally, the crystal structure is used to analyze the potential effect of the I422T mutation in δ-COP previously reported to cause a neurodegenerative phenotype in mice.

Articles - 4o8q mentioned but not cited (3)

  1. 9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments. Dodonova SO, Aderhold P, Kopp J, Ganeva I, Röhling S, Hagen WJH, Sinning I, Wieland F, Briggs JAG. Elife 6 e26691 (2017)
  2. Recycling of Golgi glycosyltransferases requires direct binding to coatomer. Liu L, Doray B, Kornfeld S. Proc Natl Acad Sci U S A 115 8984-8989 (2018)
  3. Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 μ homology domain. Shimada A, Yamaguchi A, Kohda D. Sci Rep 6 19565 (2016)


Reviews citing this publication (1)

  1. Formation of COPI-coated vesicles at a glance. Arakel EC, Schwappach B. J Cell Sci 131 jcs209890 (2018)

Articles citing this publication (2)

  1. Structural basis for the binding of tryptophan-based motifs by δ-COP. Suckling RJ, Poon PP, Travis SM, Majoul IV, Hughson FM, Evans PR, Duden R, Owen DJ. Proc Natl Acad Sci U S A 112 14242-14247 (2015)
  2. δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function. Arakel EC, Richter KP, Clancy A, Schwappach B. Proc Natl Acad Sci U S A 113 6916-6921 (2016)


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