2A6M

Crystal Structure of the ISHp608 Transposase

2A6M の概要

• エントリーDOI: 10.2210/pdb2a6m/pdb
• 関連するPDBエントリー: 2A6O
• 分子名称: ISHp608 transposase (2 entities in total)
• 機能のキーワード: rna recognition motif, transcription-dna complex, transcription/dna
• 由来する生物種: Helicobacter pylori
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36212.29

構造登録者

Ronning, D.R.,Guynet, C.,Ton-Hoang, B.,Perez, Z.N.,Ghirlando, R.,Chandler, M.,Dyda, F. (登録日: 2005-07-03, 公開日: 2005-10-25, 最終更新日: 2024-02-14)

主引用文献

Ronning, D.R.,Guynet, C.,Ton-Hoang, B.,Perez, Z.N.,Ghirlando, R.,Chandler, M.,Dyda, F.
Active site sharing and subterminal hairpin recognition in a new class of DNA transposases.
Mol.Cell, 20:143-154, 2005

PubMed Abstract: Many bacteria harbor simple transposable elements termed insertion sequences (IS). In Helicobacter pylori, the chimeric IS605 family elements are particularly interesting due to their proximity to genes encoding gastric epithelial invasion factors. Protein sequences of IS605 transposases do not bear the hallmarks of other well-characterized transposases. We have solved the crystal structure of full-length transposase (TnpA) of a representative member, ISHp608. Structurally, TnpA does not resemble any characterized transposase; rather, it is related to rolling circle replication (RCR) proteins. Consistent with RCR, Mg2+ and a conserved tyrosine, Tyr127, are essential for DNA nicking and the formation of a covalent intermediate between TnpA and DNA. TnpA is dimeric, contains two shared active sites, and binds two DNA stem loops representing the conserved inverted repeats near each end of ISHp608. The cocrystal structure with stem-loop DNA illustrates how this family of transposases specifically recognizes and pairs ends, necessary steps during transposition.

PubMed: 16209952
DOI: 10.1016/j.molcel.2005.07.026

実験手法

X-RAY DIFFRACTION (2.4 Å)