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| <StructureSection load='4xlg' size='340' side='right'caption='[[4xlg]], [[Resolution|resolution]] 1.78Å' scene=''> | | <StructureSection load='4xlg' size='340' side='right'caption='[[4xlg]], [[Resolution|resolution]] 1.78Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4xlg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canga Canga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XLG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xlg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata_CBS_138 Candida glabrata CBS 138]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XLG FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLX4, CAGL0M04389g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284593 CANGA]), SLX1, CAGL0K06941g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284593 CANGA])</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=4xlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlg OCA], [https://pdbe.org/4xlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xlg RCSB], [https://www.ebi.ac.uk/pdbsum/4xlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlg 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=4xlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlg OCA], [http://pdbe.org/4xlg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xlg RCSB], [http://www.ebi.ac.uk/pdbsum/4xlg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlg ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/SLX4_CANGA SLX4_CANGA]] Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. [[http://www.uniprot.org/uniprot/SLX1_CANGA SLX1_CANGA]] Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. | + | [https://www.uniprot.org/uniprot/SLX4_CANGA SLX4_CANGA] Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | |
| ==See Also== | | ==See Also== |
- | *[[Endonuclease|Endonuclease]] | + | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Canga]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Gaur, V]] | + | [[Category: Gaur V]] |
- | [[Category: Gorecka, K M]] | + | [[Category: Gorecka KM]] |
- | [[Category: Komorowska, W]] | + | [[Category: Komorowska W]] |
- | [[Category: Nowotny, M]] | + | [[Category: Nowotny M]] |
- | [[Category: Sanctis, D de]]
| + | [[Category: Szczepanowski RH]] |
- | [[Category: Szczepanowski, R H]] | + | [[Category: West SC]] |
- | [[Category: West, S C]] | + | [[Category: Wyatt HDM]] |
- | [[Category: Wyatt, H D.M]] | + | [[Category: De Sanctis D]] |
- | [[Category: Dna repair]] | + | |
- | [[Category: Giy-yig]]
| + | |
- | [[Category: Homogolous recombination]]
| + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Nuclease]]
| + | |
| Structural highlights
Function
SLX4_CANGA Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Publication Abstract from PubMed
The SLX1-SLX4 endonuclease required for homologous recombination and DNA repair in eukaryotic cells cleaves a variety of branched DNA structures. The nuclease subunit SLX1 is activated by association with a scaffolding protein SLX4. At the present time, little is known about the structure of SLX1-SLX4 or its mechanism of action. Here, we report the structural insights into SLX1-SLX4 by detailing the crystal structure of Candida glabrata (Cg) Slx1 alone and in combination with the C-terminal region of Slx4. The structure of Slx1 reveals a compact arrangement of the GIY-YIG nuclease and RING domains, which is reinforced by a long alpha helix. Slx1 forms a stable homodimer that blocks its active site. Slx1-Slx4 interaction is mutually exclusive with Slx1 homodimerization, suggesting a mechanism for Slx1 activation by Slx4.
Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease.,Gaur V, Wyatt HD, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M Cell Rep. 2015 Mar 3. pii: S2211-1247(15)00165-5. doi:, 10.1016/j.celrep.2015.02.019. PMID:25753413[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gaur V, Wyatt HD, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M. Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease. Cell Rep. 2015 Mar 3. pii: S2211-1247(15)00165-5. doi:, 10.1016/j.celrep.2015.02.019. PMID:25753413 doi:http://dx.doi.org/10.1016/j.celrep.2015.02.019
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