6S7X

dARC1 capsid domain dimer, orthorhombic form at 1.7 Angstrom

6S7X の概要

• エントリーDOI: 10.2210/pdb6s7x/pdb
• 関連するPDBエントリー: 6S7Y
• 分子名称: Activity-regulated cytoskeleton associated protein 1, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: capsid retrotransposon trafficking exapted, neuropeptide
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39664.01

構造登録者

Cottee, M.A.,Taylor, I.A. (登録日: 2019-07-07, 公開日: 2020-01-15, 最終更新日: 2024-10-16)

主引用文献

Cottee, M.A.,Letham, S.C.,Young, G.R.,Stoye, J.P.,Taylor, I.A.
Structure ofDrosophila melanogasterARC1 reveals a repurposed molecule with characteristics of retroviral Gag.
Sci Adv, 6:eaay6354-eaay6354, 2020

PubMed Abstract: The tetrapod neuronal protein ARC and its homolog, dARC1, have important but differing roles in neuronal development. Both are thought to originate through exaptation of ancient Ty3/Gypsy retrotransposon Gag, with their novel function relying on an original capacity for self-assembly and encapsidation of nucleic acids. Here, we present the crystal structure of dARC1 CA and examine the relationship between dARC1, mammalian ARC, and the CA protein of circulating retroviruses. We show that while the overall architecture is highly related to that of orthoretroviral and spumaretroviral CA, there are substantial deviations in both amino- and carboxyl-terminal domains, potentially affecting recruitment of partner proteins and particle assembly. The degree of sequence and structural divergence suggests that Ty3/Gypsy Gag has been exapted on two separate occasions and that, although mammalian ARC and dARC1 share functional similarity, the structures have undergone different adaptations after appropriation into the tetrapod and insect genomes.

PubMed: 31911950
DOI: 10.1126/sciadv.aay6354

実験手法

X-RAY DIFFRACTION (1.7 Å)