2XMA

DEINOCOCCUS RADIODURANS ISDRA2 TRANSPOSASE RIGHT END DNA COMPLEX

2XMA の概要

• エントリーDOI: 10.2210/pdb2xma/pdb
• 関連するPDBエントリー: 2XM3
• 分子名称: TRANSPOSASE, DRA2 TRANSPOSASE RIGHT END RECOGNITION SITE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: dna binding protein-dna complex, transposition, mobile element, dna binding protein/dna
• 由来する生物種: DEINOCOCCUS RADIODURANS; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 107924.56

構造登録者

Hickman, A.B.,James, J.A.,Barabas, O.,Pasternak, C.,Ton-Hoang, B.,Chandler, M.,Sommer, S.,Dyda, F. (登録日: 2010-07-26, 公開日: 2010-10-13, 最終更新日: 2023-12-20)

主引用文献

Hickman, A.B.,James, J.A.,Barabas, O.,Pasternak, C.,Ton-Hoang, B.,Chandler, M.,Sommer, S.,Dyda, F.
DNA Recognition and the Precleavage State During Single-Stranded DNA Transposition in D. Radiodurans.
Embo J., 29:3840-, 2010

PubMed Abstract: Bacterial insertion sequences (ISs) from the IS200/IS605 family encode the smallest known DNA transposases and mobilize through single-stranded DNA transposition. Transposition by one particular family member, ISDra2 from Deinococcus radiodurans, is dramatically stimulated upon massive γ irradiation. We have determined the crystal structures of four ISDra2 transposase/IS end complexes; combined with in vivo activity assays and fluorescence anisotropy binding measurements, these have revealed the molecular basis of strand discrimination and transposase action. The structures also show that previously established structural rules of target site recognition that allow different specific sequences to be targeted are only partially conserved among family members. Furthermore, we have captured a fully assembled active site including the scissile phosphate bound by a divalent metal ion cofactor (Cd²(+)) that supports DNA cleavage. Finally, the observed active site rearrangements when the transposase binds a metal ion in which it is inactive provide a clear rationale for metal ion specificity.

PubMed: 20890269
DOI: 10.1038/EMBOJ.2010.241

実験手法

X-RAY DIFFRACTION (2.3 Å)