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4R79

Mos1 transposase paired-end complex with left transposon end

4R79 の概要
エントリーDOI10.2210/pdb4r79/pdb
関連するPDBエントリー2F7T 3HOS 3HOT 4U7B
分子名称left Inverted repeat NTS, left Inverted repeat TS, left Inverted repeat NTS H, ... (7 entities in total)
機能のキーワードtransposase, protein-dna complex, transpososome, rnase-h like catalytic fold helix-turn-helix, dna transposition, dna cleavage, dna integration, transposon, inverted repeats, recombination-dna complex, recombination/dna
由来する生物種Drosophila mauritiana (Fruit fly)
詳細
細胞内の位置Nucleus : 4R79
タンパク質・核酸の鎖数8
化学式量合計130662.03
構造登録者
Richardson, J.M. (登録日: 2014-08-27, 公開日: 2015-04-22, 最終更新日: 2024-10-16)
主引用文献Trubitsyna, M.,Grey, H.,Houston, D.R.,Finnegan, D.J.,Richardson, J.M.
Structural Basis for the Inverted Repeat Preferences of mariner Transposases.
J.Biol.Chem., 290:13531-13540, 2015
Cited by
PubMed Abstract: The inverted repeat (IR) sequences delimiting the left and right ends of many naturally active mariner DNA transposons are non-identical and have different affinities for their transposase. We have compared the preferences of two active mariner transposases, Mos1 and Mboumar-9, for their imperfect transposon IRs in each step of transposition: DNA binding, DNA cleavage, and DNA strand transfer. A 3.1 Å resolution crystal structure of the Mos1 paired-end complex containing the pre-cleaved left IR sequences reveals the molecular basis for the reduced affinity of the Mos1 transposase DNA-binding domain for the left IR as compared with the right IR. For both Mos1 and Mboumar-9, in vitro DNA transposition is most efficient when the preferred IR sequence is present at both transposon ends. We find that this is due to the higher efficiency of cleavage and strand transfer of the preferred transposon end. We show that the efficiency of Mboumar-9 transposition is improved almost 4-fold by changing the 3' base of the preferred Mboumar-9 IR from guanine to adenine. This preference for adenine at the reactive 3' end for both Mos1 and Mboumar-9 may be a general feature of mariner transposition.
PubMed: 25869132
DOI: 10.1074/jbc.M115.636704
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.1 Å)
構造検証レポート
Validation report summary of 4r79
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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