4xm5: Difference between revisions
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''' | ==C. glabrata Slx1.== | ||
<StructureSection load='4xm5' size='340' side='right' caption='[[4xm5]], [[Resolution|resolution]] 2.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xm5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XM5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XM5 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=4xm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xm5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xm5 RCSB], [http://www.ebi.ac.uk/pdbsum/4xm5 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gaur, V]] | [[Category: Gaur, V]] | ||
[[Category: Gorecka, K | [[Category: Gorecka, K M]] | ||
[[Category: Komorowska, W]] | |||
[[Category: Nowotny, M]] | [[Category: Nowotny, M]] | ||
[[Category: | [[Category: Sanctis, D de]] | ||
[[Category: | [[Category: Szczepanowski, R H]] | ||
[[Category: West, S | [[Category: West, S C]] | ||
[[Category: Wyatt, H | [[Category: Wyatt, H D.M]] | ||
[[Category: | [[Category: Dna repair]] | ||
[[Category: Giy-yig]] | |||
[[Category: Homogolous recombination]] | |||
[[Category: Hydrolase]] | |||
[[Category: Nuclease]] | |||
Revision as of 16:57, 26 March 2015
C. glabrata Slx1.C. glabrata Slx1.
Structural highlights
Function[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. Publication Abstract from PubMedThe 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. References
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