3r7p

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Current revision (12:13, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3r7p' size='340' side='right'caption='[[3r7p]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3r7p' size='340' side='right'caption='[[3r7p]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r7p]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_58100 Atcc 58100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R7P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r7p]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptographium_truncatum Leptographium truncatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R7P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.704&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rps3/HEG fusion ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330483 ATCC 58100])</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>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </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=3r7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r7p OCA], [https://pdbe.org/3r7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r7p RCSB], [https://www.ebi.ac.uk/pdbsum/3r7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r7p ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r7p OCA], [https://pdbe.org/3r7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r7p RCSB], [https://www.ebi.ac.uk/pdbsum/3r7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r7p 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/C7SWF3_9PEZI C7SWF3_9PEZI]
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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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<div class="pdbe-citations 3r7p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 58100]]
 
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[[Category: Deoxyribonuclease I]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Edgell, D R]]
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[[Category: Leptographium truncatum]]
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[[Category: Mak, A N.S]]
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[[Category: Edgell DR]]
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[[Category: Stoddard, B L]]
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[[Category: Mak ANS]]
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[[Category: Takeuchi, R]]
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[[Category: Stoddard BL]]
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[[Category: Gene therapy]]
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[[Category: Takeuchi R]]
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[[Category: Homing endonuclease]]
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[[Category: Hydrolase-dna complex]]
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Current revision

The crystal structure of I-LtrI

PDB ID 3r7p

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