3QQY
Crystal structure of a novel LAGLIDADG homing endonuclease, I-OnuI (from Ophiostoma novo-ulmi subsp. americana)
Summary for 3QQY
| Entry DOI | 10.2210/pdb3qqy/pdb |
| Descriptor | Ribosomal protein 3/homing endonuclease-like protein fusion, DNA (26-MER), MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | protein-dna comlex, laglidadg family, hydrolase, dna binding, mitochondrion, hydrolase-dna complex, hydrolase/dna |
| Biological source | Ophiostoma novo-ulmi subsp. americana More |
| Total number of polymer chains | 3 |
| Total formula weight | 51171.52 |
| Authors | Takeuchi, R.,Stoddard, B.L. (deposition date: 2011-02-16, release date: 2011-07-20, Last modification date: 2023-09-13) |
| Primary citation | 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 Cited by 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: 21784983DOI: 10.1073/pnas.1107719108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.401 Å) |
Structure validation
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