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| | <StructureSection load='4yis' size='340' side='right'caption='[[4yis]], [[Resolution|resolution]] 2.89Å' scene=''> | | <StructureSection load='4yis' size='340' side='right'caption='[[4yis]], [[Resolution|resolution]] 2.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yis]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Crypa Crypa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YIS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YIS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yis]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YIS 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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yit|4yit]]</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=4yis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yis OCA], [https://pdbe.org/4yis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yis RCSB], [https://www.ebi.ac.uk/pdbsum/4yis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yis ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mtSrRNA I4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5116 CRYPA])</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=4yis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yis OCA], [http://pdbe.org/4yis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yis RCSB], [http://www.ebi.ac.uk/pdbsum/4yis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yis ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O20960_CRYPA O20960_CRYPA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Crypa]] | + | [[Category: Cryphonectria parasitica]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hallinan, J P]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Kaiser, B K]] | + | [[Category: Hallinan JP]] |
| - | [[Category: Stoddard, B L]] | + | [[Category: Kaiser BK]] |
| - | [[Category: Homing endonuclease]] | + | [[Category: Stoddard BL]] |
| - | [[Category: Hydrolase-dna complex]]
| + | |
| - | [[Category: Laglidadg]]
| + | |
| - | [[Category: Meganuclease]]
| + | |
| Structural highlights
Function
O20960_CRYPA
Publication Abstract from PubMed
LAGLIDADG meganucleases are DNA cleaving enzymes used for genome engineering. While their cleavage specificity can be altered using several protein engineering and selection strategies, their overall targetability is limited by highly specific indirect recognition of the central four base pairs within their recognition sites. In order to examine the physical basis of indirect sequence recognition and to expand the number of such nucleases available for genome engineering, we have determined the target sites, DNA-bound structures, and central four cleavage fidelities of nine related enzymes. Subsequent crystallographic analyses of a meganuclease bound to two noncleavable target sites, each containing a single inactivating base pair substitution at its center, indicates that a localized slip of the mutated base pair causes a small change in the DNA backbone conformation that results in a loss of metal occupancy at one binding site, eliminating cleavage activity.
Indirect DNA Sequence Recognition and Its Impact on Nuclease Cleavage Activity.,Lambert AR, Hallinan JP, Shen BW, Chik JK, Bolduc JM, Kulshina N, Robins LI, Kaiser BK, Jarjour J, Havens K, Scharenberg AM, Stoddard BL Structure. 2016 Apr 27. pii: S0969-2126(16)30035-1. doi:, 10.1016/j.str.2016.03.024. PMID:27133026[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lambert AR, Hallinan JP, Shen BW, Chik JK, Bolduc JM, Kulshina N, Robins LI, Kaiser BK, Jarjour J, Havens K, Scharenberg AM, Stoddard BL. Indirect DNA Sequence Recognition and Its Impact on Nuclease Cleavage Activity. Structure. 2016 Apr 27. pii: S0969-2126(16)30035-1. doi:, 10.1016/j.str.2016.03.024. PMID:27133026 doi:http://dx.doi.org/10.1016/j.str.2016.03.024
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