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4D1Q

Hermes transposase bound to its terminal inverted repeat

4D1Q の概要
エントリーDOI10.2210/pdb4d1q/pdb
分子名称TRANSPOSASE, TERMINAL INVERTED REPEAT, SODIUM ION, ... (4 entities in total)
機能のキーワードtransposition, protein-dna complex, tranpososome, hat
由来する生物種MUSCA DOMESTICA (HOUSE FLY)
詳細
タンパク質・核酸の鎖数12
化学式量合計283377.39
構造登録者
Hickman, A.B.,Ewis, H.,Li, X.,Knapp, J.,Laver, T.,Doss, A.L.,Tolun, G.,Steven, A.,Grishaev, A.,Bax, A.,Atkinson, P.,Craig, N.L.,Dyda, F. (登録日: 2014-05-04, 公開日: 2014-07-30, 最終更新日: 2024-05-08)
主引用文献Hickman, A.B.,Ewis, H.E.,Li, X.,Knapp, J.A.,Laver, T.,Doss, A.,Tolun, G.,Steven, A.C.,Grishaev, A.,Bax, A.,Atkinson, P.W.,Craig, N.L.,Dyda, F.
Structural Basis of Hat Transposon End Recognition by Hermes, an Octameric DNA Transposase from Musca Domestica.
Cell(Cambridge,Mass.), 158:353-, 2014
Cited by
PubMed Abstract: Hermes is a member of the hAT transposon superfamily that has active representatives, including McClintock's archetypal Ac mobile genetic element, in many eukaryotic species. The crystal structure of the Hermes transposase-DNA complex reveals that Hermes forms an octameric ring organized as a tetramer of dimers. Although isolated dimers are active in vitro for all the chemical steps of transposition, only octamers are active in vivo. The octamer can provide not only multiple specific DNA-binding domains to recognize repeated subterminal sequences within the transposon ends, which are important for activity, but also multiple nonspecific DNA binding surfaces for target capture. The unusual assembly explains the basis of bipartite DNA recognition at hAT transposon ends, provides a rationale for transposon end asymmetry, and suggests how the avidity provided by multiple sites of interaction could allow a transposase to locate its transposon ends amidst a sea of chromosomal DNA.
PubMed: 25036632
DOI: 10.1016/J.CELL.2014.05.037
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.4 Å)
構造検証レポート
Validation report summary of 4d1q
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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