3QQY

Crystal structure of a novel LAGLIDADG homing endonuclease, I-OnuI (from Ophiostoma novo-ulmi subsp. americana)

3QQY の概要

• エントリーDOI: 10.2210/pdb3qqy/pdb
• 分子名称: Ribosomal protein 3/homing endonuclease-like protein fusion, DNA (26-MER), MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: protein-dna comlex, laglidadg family, hydrolase, dna binding, mitochondrion, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Ophiostoma novo-ulmi subsp. americana; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 51171.52

構造登録者

Takeuchi, R.,Stoddard, B.L. (登録日: 2011-02-16, 公開日: 2011-07-20, 最終更新日: 2023-09-13)

主引用文献

Takeuchi, R.,Lambert, A.R.,Mak, A.N.,Jacoby, K.,Dickson, R.J.,Gloor, G.B.,Scharenberg, A.M.,Edgell, D.R.,Stoddard, B.L.
Tapping natural reservoirs of homing endonucleases for targeted gene modification.
Proc.Natl.Acad.Sci.USA, 108:13077-13082, 2011

PubMed Abstract: Homing endonucleases mobilize their own genes by generating double-strand breaks at individual target sites within potential host DNA. Because of their high specificity, these proteins are used for "genome editing" in higher eukaryotes. However, alteration of homing endonuclease specificity is quite challenging. Here we describe the identification and phylogenetic analysis of over 200 naturally occurring LAGLIDADG homing endonucleases (LHEs). Biochemical and structural characterization of endonucleases from one clade within the phylogenetic tree demonstrates strong conservation of protein structure contrasted against highly diverged DNA target sites and indicates that a significant fraction of these proteins are sufficiently stable and active to serve as engineering scaffolds. This information was exploited to create a targeting enzyme to disrupt the endogenous monoamine oxidase B gene in human cells. The ubiquitous presence and diversity of LHEs described in this study may facilitate the creation of many tailored nucleases for genome editing.

PubMed: 21784983
DOI: 10.1073/pnas.1107719108

実験手法

X-RAY DIFFRACTION (2.401 Å)