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| | <StructureSection load='5a0m' size='340' side='right'caption='[[5a0m]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='5a0m' size='340' side='right'caption='[[5a0m]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a0m]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A0M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a0m]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] 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=5A0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCEI, OMEGA, SECY, Q0160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=5a0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0m OCA], [https://pdbe.org/5a0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0m RCSB], [https://www.ebi.ac.uk/pdbsum/5a0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0m 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=5a0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0m OCA], [http://pdbe.org/5a0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a0m RCSB], [http://www.ebi.ac.uk/pdbsum/5a0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SCE1_YEAST SCE1_YEAST]] Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the 21S rRNA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Specifically recognizes and cleaves the sequence 5'-TAGGGATAACAGGGTAAT-3'. | + | [https://www.uniprot.org/uniprot/SCE1_YEAST SCE1_YEAST] Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the 21S rRNA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Specifically recognizes and cleaves the sequence 5'-TAGGGATAACAGGGTAAT-3'. |
| | <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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blanco, F J]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Merino, N]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Molina, R]] | + | [[Category: Blanco FJ]] |
| - | [[Category: Prieto, J]] | + | [[Category: Merino N]] |
| - | [[Category: Redondo, P]] | + | [[Category: Molina R]] |
| - | [[Category: Villate, M]] | + | [[Category: Prieto J]] |
| - | [[Category: Gene targeting]] | + | [[Category: Redondo P]] |
| - | [[Category: Genetic]] | + | [[Category: Villate M]] |
| - | [[Category: Homing endonuclease]]
| + | |
| - | [[Category: Hydrolase-dna complex]]
| + | |
| - | [[Category: Protein-dna interaction]]
| + | |
| Structural highlights
Function
SCE1_YEAST Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the 21S rRNA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Specifically recognizes and cleaves the sequence 5'-TAGGGATAACAGGGTAAT-3'.
Publication Abstract from PubMed
Homing endonucleases are highly specific DNA-cleaving enzymes that recognize and cleave long stretches of DNA. The engineering of these enzymes provides instruments for genome modification in a wide range of fields, including gene targeting. The homing endonuclease I-SceI from the yeast Saccharomyces cerevisiae has been purified after overexpression in Escherichia coli and its crystal structure has been determined in complex with its target DNA. In order to evaluate the number of ions that are involved in the cleavage process, thus determining the catalytic mechanism, crystallization experiments were performed in the presence of Mn(2+), yielding crystals that were suitable for X-ray diffraction analysis. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 80.11, b = 80.57, c = 130.87 A, alpha = beta = gamma = 90 degrees . The self-rotation function and the Matthews coefficient suggested the presence of two protein-DNA complexes in the asymmetric unit. The crystals diffracted to a resolution limit of 2.9 A using synchrotron radiation. From the anomalous data, it was determined that three cations are involved in catalysis and it was confirmed that I-SceI follows a two-metal-ion DNA-strand cleavage mechanism.
Structure of the I-SceI nuclease complexed with its dsDNA target and three catalytic metal ions.,Prieto J, Redondo P, Merino N, Villate M, Montoya G, Blanco FJ, Molina R Acta Crystallogr F Struct Biol Commun. 2016 Jun 1;72(Pt 6):473-9. doi:, 10.1107/S2053230X16007512. Epub 2016 May 23. PMID:27303901[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Prieto J, Redondo P, Merino N, Villate M, Montoya G, Blanco FJ, Molina R. Structure of the I-SceI nuclease complexed with its dsDNA target and three catalytic metal ions. Acta Crystallogr F Struct Biol Commun. 2016 Jun 1;72(Pt 6):473-9. doi:, 10.1107/S2053230X16007512. Epub 2016 May 23. PMID:27303901 doi:http://dx.doi.org/10.1107/S2053230X16007512
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