4U7B

Crystal structure of a pre-cleavage Mos1 transpososome

4U7B の概要

• エントリーDOI: 10.2210/pdb4u7b/pdb
• 関連するPDBエントリー: 2F7T 3HOS 3HOT
• 分子名称: DNA (25-MER), DNA (31-MER), Mariner Mos1 transposase, ... (5 entities in total)
• 機能のキーワード: transposase, transposon synaptic complex, helix-turn-helix, rnase-h like fold, dna transposition, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Drosophila mauritiana; 詳細
• 細胞内の位置: Nucleus : Q7JQ07
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 173577.60

構造登録者

Richardson, J.M. (登録日: 2014-07-30, 公開日: 2015-02-11, 最終更新日: 2024-11-06)

主引用文献

Dornan, J.,Grey, H.,Richardson, J.M.
Structural role of the flanking DNA in mariner transposon excision.
Nucleic Acids Res., 43:2424-2432, 2015

PubMed Abstract: During cut-and-paste mariner/Tc1 transposition, transposon DNA is cut precisely at its junction with flanking DNA, ensuring the transposon is neither shortened nor lengthened with each transposition event. Each transposon end is flanked by a TpA dinucleotide: the signature target site duplication of mariner/Tc1 transposition. To establish the role of this sequence in accurate DNA cleavage, we have determined the crystal structure of a pre-second strand cleavage mariner Mos1 transpososome. The structure reveals the route of an intact DNA strand through the transposase active site before second strand cleavage. The crossed architecture of this pre-second strand cleavage paired-end complex supports our proposal that second strand cleavage occurs in trans. The conserved mariner transposase WVPHEL and YSPDL motifs position the strand for accurate DNA cleavage. Base-specific recognition of the flanking DNA by conserved amino acids is revealed, defining a new role for the WVPHEL motif in mariner transposition and providing a molecular explanation for in vitro mutagenesis data. Comparison of the pre-TS cleavage and post-cleavage Mos1 transpososomes with structures of Prototype Foamy Virus intasomes suggests a binding mode for target DNA prior to Mos1 transposon integration.

PubMed: 25662605
DOI: 10.1093/nar/gkv096

実験手法

X-RAY DIFFRACTION (3.09 Å)