4O8Q

Crystal structure of bovine MHD domain of the COPI delta subunit at 2.15 A resolution

4O8Q の概要

• エントリーDOI: 10.2210/pdb4o8q/pdb
• 分子名称: Coatomer subunit delta, FORMIC ACID (3 entities in total)
• 機能のキーワード: mhd, protein transport
• 由来する生物種: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• 細胞内の位置: Cytoplasm : P53619
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55214.51

構造登録者

Lahav, A.,Rozenberg, H.,Cassel, D.,Adir, N. (登録日: 2013-12-29, 公開日: 2015-01-07, 最終更新日: 2024-04-03)

主引用文献

Lahav, A.,Rozenberg, H.,Parnis, A.,Cassel, D.,Adir, N.
Structure of the bovine COPI delta subunit mu homology domain at 2.15 angstrom resolution.
Acta Crystallogr.,Sect.D, 71:1328-1334, 2015

PubMed 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.

PubMed: 26057672
DOI: 10.1107/S1399004715006203

実験手法

X-RAY DIFFRACTION (2.15 Å)