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3qqy

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==Crystal structure of a novel LAGLIDADG homing endonuclease, I-OnuI (from Ophiostoma novo-ulmi subsp. americana)==
==Crystal structure of a novel LAGLIDADG homing endonuclease, I-OnuI (from Ophiostoma novo-ulmi subsp. americana)==
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<StructureSection load='3qqy' size='340' side='right' caption='[[3qqy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='3qqy' size='340' side='right'caption='[[3qqy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qqy]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QQY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qqy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ophiostoma_novo-ulmi_subsp._americana Ophiostoma novo-ulmi subsp. americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QQY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.401&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rps3/HEG fusion ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2759 Eukaryota])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qqy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qqy RCSB], [http://www.ebi.ac.uk/pdbsum/3qqy PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qqy OCA], [https://pdbe.org/3qqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qqy RCSB], [https://www.ebi.ac.uk/pdbsum/3qqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qqy ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q4VWW5_OPHNO Q4VWW5_OPHNO]
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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.
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Tapping natural reservoirs of homing endonucleases for targeted gene modification.,Takeuchi R, Lambert AR, Mak AN, Jacoby K, Dickson RJ, Gloor GB, Scharenberg AM, Edgell DR, Stoddard BL Proc Natl Acad Sci U S A. 2011 Jul 22. PMID:21784983<ref>PMID:21784983</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eukaryota]]
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[[Category: Large Structures]]
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[[Category: Stoddard, B L]]
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[[Category: Ophiostoma novo-ulmi subsp. americana]]
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[[Category: Takeuchi, R]]
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[[Category: Stoddard BL]]
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[[Category: Dna binding]]
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[[Category: Takeuchi R]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-dna complex]]
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[[Category: Laglidadg family]]
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[[Category: Mitochondrion]]
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[[Category: Protein-dna comlex]]
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Current revision

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

PDB ID 3qqy

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