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| | <StructureSection load='5e5o' size='340' side='right'caption='[[5e5o]], [[Resolution|resolution]] 2.36Å' scene=''> | | <StructureSection load='5e5o' size='340' side='right'caption='[[5e5o]], [[Resolution|resolution]] 2.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e5o]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Sormk Sormk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E5O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e5o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sordaria_macrospora_k-hell Sordaria macrospora k-hell] 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=5E5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E5O 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lox|4lox]], [[5e5p|5e5p]], [[5e5s|5e5s]], [[5e63|5e63]], [[5e67|5e67]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMAC_12671 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=771870 SORMK])</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=5e5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5o OCA], [https://pdbe.org/5e5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e5o RCSB], [https://www.ebi.ac.uk/pdbsum/5e5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5o ProSAT]</span></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=5e5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5o OCA], [http://pdbe.org/5e5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e5o RCSB], [http://www.ebi.ac.uk/pdbsum/5e5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F7WD42_SORMK F7WD42_SORMK] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sormk]] | + | [[Category: Sordaria macrospora k-hell]] |
| - | [[Category: Shen, B W]]
| + | [[Category: Synthetic construct]] |
| - | [[Category: Complex]]
| + | [[Category: Shen BW]] |
| - | [[Category: Hydrolase-dna complex]]
| + | |
| - | [[Category: I-smami]] | + | |
| - | [[Category: Laglidadg]] | + | |
| - | [[Category: Uncleaved]]
| + | |
| Structural highlights
Function
F7WD42_SORMK
Publication Abstract from PubMed
LAGLIDADG homing endonucleases ("meganucleases") are highly specific DNA cleaving enzymes that are used for genome engineering. Like other enzymes that act on DNA targets, meganucleases often display binding affinities and cleavage activities that are dominated by one protein domain. To decipher the underlying mechanism of asymmetric DNA recognition and catalysis, we identified and characterized a new monomeric meganuclease (I-SmaMI), which belongs to a superfamily of homologous enzymes that recognize divergent DNA sequences. We solved a series of crystal structures of the enzyme-DNA complex representing a progression of sequential reaction states, and we compared the structural rearrangements and surface potential distributions within each protein domain against their relative contribution to binding affinity. We then determined the effects of equivalent point mutations in each of the two enzyme active sites to determine whether asymmetry in DNA recognition is translated into corresponding asymmetry in DNA cleavage activity. These experiments demonstrate the structural basis for "dominance" by one protein domain over the other and provide insights into this enzyme's conformational switch from a nonspecific search mode to a more specific recognition mode.
The Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease.,Shen BW, Lambert A, Walker BC, Stoddard BL, Kaiser BK J Mol Biol. 2015 Dec 15. pii: S0022-2836(15)00696-8. doi:, 10.1016/j.jmb.2015.12.005. PMID:26705195[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shen BW, Lambert A, Walker BC, Stoddard BL, Kaiser BK. The Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease. J Mol Biol. 2015 Dec 15. pii: S0022-2836(15)00696-8. doi:, 10.1016/j.jmb.2015.12.005. PMID:26705195 doi:http://dx.doi.org/10.1016/j.jmb.2015.12.005
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