2VJU

Crystal structure of the IS608 transposase in complex with the complete Right end 35-mer DNA and manganese

2VJU の概要

• エントリーDOI: 10.2210/pdb2vju/pdb
• 分子名称: TRANSPOSASE ORFA, RIGHT END 35-MER, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: protein-dna complex, dna-binding protein, huh motif, dna stem loop, transposition, dna binding protein
• 由来する生物種: HELICOBACTER PYLORI; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 58555.59

構造登録者

Barabas, O.,Ronning, D.R.,Guynet, C.,Hickman, A.B.,Ton-Hoang, B.,Chandler, M.,Dyda, F. (登録日: 2007-12-13, 公開日: 2008-02-19, 最終更新日: 2023-12-13)

主引用文献

Barabas, O.,Ronning, D.R.,Guynet, C.,Hickman, A.B.,Ton-Hoang, B.,Chandler, M.,Dyda, F.
Mechanism of is200/is605 Family DNA Transposases: Activation and Transposon-Directed Target Site Selection.
Cell(Cambridge,Mass.), 132:208-, 2008

PubMed Abstract: The smallest known DNA transposases are those from the IS200/IS605 family. Here we show how the interplay of protein and DNA activates TnpA, the Helicobacter pylori IS608 transposase, for catalysis. First, transposon end binding causes a conformational change that aligns catalytically important protein residues within the active site. Subsequent precise cleavage at the left and right ends, the steps that liberate the transposon from its donor site, does not involve a site-specific DNA-binding domain. Rather, cleavage site recognition occurs by complementary base pairing with a TnpA-bound subterminal transposon DNA segment. Thus, the enzyme active site is constructed from elements of both protein and DNA, reminiscent of the interdependence of protein and RNA in the ribosome. Our structural results explain why the transposon ends are asymmetric and how the transposon selects a target site for integration, and they allow us to propose a molecular model for the entire transposition reaction.

PubMed: 18243097
DOI: 10.1016/J.CELL.2007.12.029

実験手法

X-RAY DIFFRACTION (2.4 Å)