7NLI

S. cerevisiae Ty1 p22 restriction factor, Gag CA-CTD, AUG2 variant

7NLI の概要

• エントリーDOI: 10.2210/pdb7nli/pdb
• 関連するPDBエントリー: 7NLG 7NLH
• 分子名称: Ty1 Gag p22 (1 entity in total)
• 機能のキーワード: restriction factor, ty1, gag, ca, virus like particle
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 37294.18

構造登録者

Cottee, M.A.,Letham, S.C.,Taylor, I.A. (登録日: 2021-02-22, 公開日: 2021-10-06, 最終更新日: 2024-10-23)

主引用文献

Cottee, M.A.,Beckwith, S.L.,Letham, S.C.,Kim, S.J.,Young, G.R.,Stoye, J.P.,Garfinkel, D.J.,Taylor, I.A.
Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control.
Nat Commun, 12:5590-5590, 2021

PubMed Abstract: Excessive replication of Saccharomyces cerevisiae Ty1 retrotransposons is regulated by Copy Number Control, a process requiring the p22/p18 protein produced from a sub-genomic transcript initiated within Ty1 GAG. In retrotransposition, Gag performs the capsid functions required for replication and re-integration. To minimize genomic damage, p22/p18 interrupts virus-like particle function by interaction with Gag. Here, we present structural, biophysical and genetic analyses of p18m, a minimal fragment of Gag that restricts transposition. The 2.8 Å crystal structure of p18m reveals an all α-helical protein related to mammalian and insect ARC proteins. p18m retains the capacity to dimerise in solution and the crystal structures reveal two exclusive dimer interfaces. We probe our findings through biophysical analysis of interface mutants as well as Ty1 transposition and p18m restriction in vivo. Our data provide insight into Ty1 Gag structure and suggest how p22/p18 might function in restriction through a blocking-of-assembly mechanism.

PubMed: 34552077
DOI: 10.1038/s41467-021-25849-0

実験手法

X-RAY DIFFRACTION (3.119 Å)