2V0R

crystal structure of a hairpin exchange variant (LTx) of the targeting LINE-1 retrotransposon endonuclease

2V0R の概要

• エントリーDOI: 10.2210/pdb2v0r/pdb
• 関連するPDBエントリー: 1VYB 2V0S
• 分子名称: LTX, SULFATE ION (3 entities in total)
• 機能のキーワード: ape-1 type, endonuclease, retrotransposition, retrotransposon, protein engineering, transcription
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55299.38

構造登録者

Repanas, K.,Zingler, N.,Layer, L.E.,Schumann, G.G.,Perrakis, A.,Weichenrieder, O. (登録日: 2007-05-17, 公開日: 2007-07-17, 最終更新日: 2023-12-13)

主引用文献

Repanas, K.,Zingler, N.,Layer, L.E.,Schumann, G.G.,Perrakis, A.,Weichenrieder, O.
Determinants for DNA Target Structure Selectivity of the Human Line-1 Retrotransposon Endonuclease
Nucleic Acids Res., 35:4914-, 2007

PubMed Abstract: The human LINE-1 endonuclease (L1-EN) is the targeting endonuclease encoded by the human LINE-1 (L1) retrotransposon. L1-EN guides the genomic integration of new L1 and Alu elements that presently account for approximately 28% of the human genome. L1-EN bears considerable technological interest, because its target selectivity may ultimately be engineered to allow the site-specific integration of DNA into defined genomic locations. Based on the crystal structure, we generated L1-EN mutants to analyze and manipulate DNA target site recognition. Crystal structures and their dynamic and functional analysis show entire loop grafts to be feasible, resulting in altered specificity, while individual point mutations do not change the nicking pattern of L1-EN. Structural parameters of the DNA target seem more important for recognition than the nucleotide sequence, and nicking profiles on DNA oligonucleotides in vitro are less well defined than the respective integration site consensus in vivo. This suggests that additional factors other than the DNA nicking specificity of L1-EN contribute to the targeted integration of non-LTR retrotransposons.

PubMed: 17626046
DOI: 10.1093/NAR/GKM516

実験手法

X-RAY DIFFRACTION (2.3 Å)