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| | <StructureSection load='2i3p' size='340' side='right'caption='[[2i3p]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2i3p' size='340' side='right'caption='[[2i3p]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2i3p]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I3P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2i3p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I3P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2i3q|2i3q]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <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=2i3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3p OCA], [http://pdbe.org/2i3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i3p RCSB], [http://www.ebi.ac.uk/pdbsum/2i3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3p 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=2i3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3p OCA], [https://pdbe.org/2i3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3p RCSB], [https://www.ebi.ac.uk/pdbsum/2i3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNE1_CHLRE DNE1_CHLRE]] Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site. | + | [https://www.uniprot.org/uniprot/DNE1_CHLRE DNE1_CHLRE] Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rosen, L]] | + | [[Category: Rosen L]] |
| - | [[Category: Sussman, D]] | + | [[Category: Sussman D]] |
| - | [[Category: Dna]]
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| - | [[Category: Homing endonulease i-crei]]
| + | |
| - | [[Category: Hydrolase-dna complex]]
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| Structural highlights
Function
DNE1_CHLRE Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Homing endonucleases are highly specific enzymes, capable of recognizing and cleaving unique DNA sequences in complex genomes. Since such DNA cleavage events can result in targeted allele-inactivation and/or allele-replacement in vivo, the ability to engineer homing endonucleases matched to specific DNA sequences of interest would enable powerful and precise genome manipulations. We have taken a step-wise genetic approach in analyzing individual homing endonuclease I-CreI protein/DNA contacts, and describe here novel interactions at four distinct target site positions. Crystal structures of two mutant endonucleases reveal the molecular interactions responsible for their altered DNA target specificities. We also combine novel contacts to create an endonuclease with the predicted target specificity. These studies provide important insights into engineering homing endonucleases with novel target specificities, as well as into the evolution of DNA recognition by this fascinating family of proteins.
Homing endonuclease I-CreI derivatives with novel DNA target specificities.,Rosen LE, Morrison HA, Masri S, Brown MJ, Springstubb B, Sussman D, Stoddard BL, Seligman LM Nucleic Acids Res. 2006;34(17):4791-800. Epub 2006 Sep 13. PMID:16971456[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rosen LE, Morrison HA, Masri S, Brown MJ, Springstubb B, Sussman D, Stoddard BL, Seligman LM. Homing endonuclease I-CreI derivatives with novel DNA target specificities. Nucleic Acids Res. 2006;34(17):4791-800. Epub 2006 Sep 13. PMID:16971456 doi:10.1093/nar/gkl645
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