View source for 4xlg

==C. glabrata Slx1 in complex with Slx4CCD.==
<StructureSection load='4xlg' size='340' side='right' caption='[[4xlg]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xlg]] is a 2 chain structure. 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>
</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>
<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://www.rcsb.org/pdb/explore.do?structureId=4xlg RCSB], [http://www.ebi.ac.uk/pdbsum/4xlg PDBsum]</span></td></tr>
</table>
== 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. 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25753413</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gaur, V]]
[[Category: Gorecka, K M]]
[[Category: Komorowska, W]]
[[Category: Nowotny, M]]
[[Category: Sanctis, D de]]
[[Category: Szczepanowski, R H]]
[[Category: West, S C]]
[[Category: Wyatt, H D.M]]
[[Category: Dna repair]]
[[Category: Giy-yig]]
[[Category: Homogolous recombination]]
[[Category: Hydrolase]]
[[Category: Nuclease]]