3MV2

Crystal Structure of a-COP in Complex with e-COP

3MV2 の概要

• エントリーDOI: 10.2210/pdb3mv2/pdb
• 関連するPDBエントリー: 3MV3
• 分子名称: Coatomer subunit alpha, Coatomer subunit epsilon (2 entities in total)
• 機能のキーワード: vesicular membrane coat coat protein complex i, protein transport
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Cytoplasm: P53622 P40509
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 215713.07

構造登録者

Hoelz, A.,Hsia, K.C. (登録日: 2010-05-03, 公開日: 2010-06-16, 最終更新日: 2024-02-21)

主引用文献

Hsia, K.C.,Hoelz, A.
Crystal structure of alpha-COP in complex with epsilon-COP provides insight into the architecture of the COPI vesicular coat.
Proc.Natl.Acad.Sci.USA, 107:11271-11276, 2010

PubMed Abstract: The heptameric coatomer complex forms the protein shell of membrane-bound vesicles that are involved in transport from the Golgi to the endoplasmatic reticulum and in intraGolgi trafficking. The heptamer can be dissected into a heterotetrameric F-subcomplex, which displays similarities to the adapter complex of the "inner" coat in clathrin-coated vesicles, and a heterotrimeric B-subcomplex, which is believed to form an "outer" coat with a morphology distinct from that of clathrin-coated vesicles. We have determined the crystal structure of the complex between the C-terminal domain (CTD) of alpha-COP and full-length epsilon-COP, two components of the B-subcomplex, at a 2.9 A resolution. The alpha-COP(CTD) x epsilon-COP heterodimer forms a rod-shaped structure, in which epsilon-COP adopts a tetratricopeptide repeat (TPR) fold that deviates substantially from the canonical superhelical conformation. The alpha-COP CTD adopts a U-shaped architecture that complements the TPR fold of epsilon-COP. The epsilon-COP TPRs form a circular bracelet that wraps around a protruding beta-hairpin of the alpha-COP CTD, thus interlocking the two proteins. The alpha-COP(CTD) x epsilon-COP complex forms heterodimers in solution, and we demonstrate biochemically that the heterodimer directly interacts with the Dsl1 tethering complex. These data suggest that the heterodimer is exposed on COPI vesicles, while the remaining part of the B-subcomplex oligomerizes underneath into a cage.

PubMed: 20534429
DOI: 10.1073/pnas.1006297107

実験手法

X-RAY DIFFRACTION (2.9 Å)