4zdt - Revision history

OCA at 09:04, 20 March 2024

OCA — Wed, 20 Mar 2024 09:04:45 GMT

←Older revision		Revision as of 09:04, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4zdt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4zdt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[https://proteopedia.org/fgij/fg.htm?mol=4zdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdt OCA], [https://pdbe.org/4zdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdt RCSB], [https://www.ebi.ac.uk/pdbsum/4zdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdt ProSAT]</span></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=4zdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdt OCA], [https://pdbe.org/4zdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdt RCSB], [https://www.ebi.ac.uk/pdbsum/4zdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/SLX1_SCHPO SLX1_SCHPO] 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. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro.[HAMAP-Rule:MF_03100]<ref>PMID:14528010</ref> <ref>PMID:15972456</ref> <ref>PMID:16467377</ref> <ref>PMID:17277362</ref> <ref>PMID:19596236</ref>		[https://www.uniprot.org/uniprot/SLX1_SCHPO SLX1_SCHPO] 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. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro.[HAMAP-Rule:MF_03100]<ref>PMID:14528010</ref> <ref>PMID:15972456</ref> <ref>PMID:16467377</ref> <ref>PMID:17277362</ref> <ref>PMID:19596236</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The SLX1-SLX4 complex is a structure-specific endonuclease that cleaves branched DNA structures and plays significant roles in DNA recombination and repair in eukaryotic cells. The heterodimeric interaction between SLX1 and SLX4 is essential for the endonuclease activity of SLX1. Here, we present the crystal structure of Slx1 C-terminal zinc finger domain in complex with the C-terminal helix-turn-helix domain of Slx4 from Schizosaccharomyces pombe at 2.0 A resolution. The structure reveals a conserved binding mechanism underling the Slx1-Slx4 interaction. Structural and sequence analyses indicate Slx1 C-terminal domain is actually an atypical C4HC3-type RING finger which normally possesses E3 ubiquitin ligase activity, but here is absolutely required for Slx1 interaction with Slx4. Furthermore, we found the C-terminal tail of S. pombe Slx1 contains a SUMO-interacting motif and can recognize Pmt3 (S. pombe SUMO), suggesting that Slx1-Slx4 complex could be recruited by SUMOylated protein targets to take part in replication associated DNA repair processes.
-
-	Crystal structure and SUMO binding of Slx1-Slx4 complex.,Lian FM, Xie S, Qian C Sci Rep. 2016 Jan 20;6:19331. doi: 10.1038/srep19331. PMID:26787556<ref>PMID:26787556</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4zdt" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 07:50, 10 May 2023

OCA — Wed, 10 May 2023 07:50:16 GMT

←Older revision		Revision as of 07:50, 10 May 2023
Line 3:		Line 3:
	<StructureSection load='4zdt' size='340' side='right'caption='[[4zdt]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4zdt' size='340' side='right'caption='[[4zdt]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4zdt]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Fission_yeast Fission yeast~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4ZDT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4zdt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">slx1, SPAP27G11.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), slx4, SPAC688.06c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=4zdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdt OCA], [https://pdbe.org/4zdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdt RCSB], [https://www.ebi.ac.uk/pdbsum/4zdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdt 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=4zdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdt OCA], [~~http~~://pdbe.org/4zdt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4zdt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4zdt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdt ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SLX1_SCHPO SLX1_SCHPO]] 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. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro.[HAMAP-Rule:MF_03100]<ref>PMID:14528010</ref> <ref>PMID:15972456</ref> <ref>PMID:16467377</ref> <ref>PMID:17277362</ref> <ref>PMID:19596236</ref> [[http://www.uniprot.org/uniprot/SLX4_SCHPO SLX4_SCHPO]] 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. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. Has Holliday junction resolvase activity in vitro. Slx4 is required for efficient processing of DNA substrates.<ref>PMID:14528010</ref> <ref>PMID:16467377</ref>	+	[https://www.uniprot.org/uniprot/SLX1_SCHPO SLX1_SCHPO] 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. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro.[HAMAP-Rule:MF_03100]<ref>PMID:14528010</ref> <ref>PMID:15972456</ref> <ref>PMID:16467377</ref> <ref>PMID:17277362</ref> <ref>PMID:19596236</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 20:

	==See Also==		==See Also==
-	*[[Endonuclease\|Endonuclease]]	+	*[[Endonuclease 3D structures\|Endonuclease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Fission yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lian, F M~~]]	+	[[Category: Schizosaccharomyces pombe 972h-]]
-	[[Category: ~~Qian, C M~~]]	+	[[Category: Lian FM]]
-	[[Category: ~~Xie, S~~]]	+	[[Category: Qian CM]]
-	[[Category: ~~Endonuclease]]~~	+	[[Category: Xie S]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ring finger~~]]	+

OCA at 07:01, 19 June 2019

OCA — Wed, 19 Jun 2019 07:01:47 GMT

←Older revision		Revision as of 07:01, 19 June 2019
Line 1:		Line 1:
		+
	==Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4==		==Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4==
-	<StructureSection load='4zdt' size='340' side='right' caption='[[4zdt]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4zdt' size='340' side='right'caption='[[4zdt]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4zdt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZDT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4zdt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZDT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4zdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdt OCA], [http://pdbe.org/4zdt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zdt RCSB], [http://www.ebi.ac.uk/pdbsum/4zdt PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">slx1, SPAP27G11.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), slx4, SPAC688.06c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=4zdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdt OCA], [http://pdbe.org/4zdt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zdt RCSB], [http://www.ebi.ac.uk/pdbsum/4zdt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4zdt" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4zdt" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Endonuclease\|Endonuclease]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Fission yeast]]
		+	[[Category: Large Structures]]
	[[Category: Lian, F M]]		[[Category: Lian, F M]]
	[[Category: Qian, C M]]		[[Category: Qian, C M]]

OCA at 15:35, 3 February 2016

OCA — Wed, 03 Feb 2016 15:35:23 GMT

←Older revision		Revision as of 15:35, 3 February 2016
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4==
		+	<StructureSection load='4zdt' size='340' side='right' caption='[[4zdt]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4zdt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZDT FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4zdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdt OCA], [http://pdbe.org/4zdt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zdt RCSB], [http://www.ebi.ac.uk/pdbsum/4zdt PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SLX1_SCHPO SLX1_SCHPO]] 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. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro.[HAMAP-Rule:MF_03100]<ref>PMID:14528010</ref> <ref>PMID:15972456</ref> <ref>PMID:16467377</ref> <ref>PMID:17277362</ref> <ref>PMID:19596236</ref> [[http://www.uniprot.org/uniprot/SLX4_SCHPO SLX4_SCHPO]] 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. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. Has Holliday junction resolvase activity in vitro. Slx4 is required for efficient processing of DNA substrates.<ref>PMID:14528010</ref> <ref>PMID:16467377</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The SLX1-SLX4 complex is a structure-specific endonuclease that cleaves branched DNA structures and plays significant roles in DNA recombination and repair in eukaryotic cells. The heterodimeric interaction between SLX1 and SLX4 is essential for the endonuclease activity of SLX1. Here, we present the crystal structure of Slx1 C-terminal zinc finger domain in complex with the C-terminal helix-turn-helix domain of Slx4 from Schizosaccharomyces pombe at 2.0 A resolution. The structure reveals a conserved binding mechanism underling the Slx1-Slx4 interaction. Structural and sequence analyses indicate Slx1 C-terminal domain is actually an atypical C4HC3-type RING finger which normally possesses E3 ubiquitin ligase activity, but here is absolutely required for Slx1 interaction with Slx4. Furthermore, we found the C-terminal tail of S. pombe Slx1 contains a SUMO-interacting motif and can recognize Pmt3 (S. pombe SUMO), suggesting that Slx1-Slx4 complex could be recruited by SUMOylated protein targets to take part in replication associated DNA repair processes.

-	~~The entry 4zdt is ON HOLD until Paper Publication~~	+	Crystal structure and SUMO binding of Slx1-Slx4 complex.,Lian FM, Xie S, Qian C Sci Rep. 2016 Jan 20;6:19331. doi: 10.1038/srep19331. PMID:26787556<ref>PMID:26787556</ref>

-	~~Authors: Lian~~, F.~~M., Wang, J.L., Xie,~~ S.~~, Qian, C.M~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4~~	+	<div class="pdbe-citations 4zdt" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Unreleased Structures~~]]	+	== References ==
-	[[Category: ~~Lian~~, F.M]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Lian, F M]]
		+	[[Category: Qian, C M]]
	[[Category: Xie, S]]		[[Category: Xie, S]]
-	[[Category: ~~Qian, C.M~~]]	+	[[Category: Endonuclease]]
-	[[Category: ~~Wang, J.L~~]]	+	[[Category: Hydrolase]]
		+	[[Category: Ring finger]]

OCA at 23:58, 30 November 2015

OCA — Mon, 30 Nov 2015 23:58:51 GMT

←Older revision		Revision as of 23:58, 30 November 2015
Line 7:		Line 7:
	Description: Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4		Description: Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Xie, S]]
-	[[Category: Wang, J.L]]
	[[Category: Lian, F.M]]		[[Category: Lian, F.M]]
		+	[[Category: Xie, S]]
	[[Category: Qian, C.M]]		[[Category: Qian, C.M]]
		+	[[Category: Wang, J.L]]

OCA at 14:17, 27 May 2015

OCA — Wed, 27 May 2015 14:17:30 GMT

←Older revision		Revision as of 14:17, 27 May 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4zdt is ON HOLD	+	The entry 4zdt is ON HOLD until Paper Publication

	Authors: Lian, F.M., Wang, J.L., Xie, S., Qian, C.M.		Authors: Lian, F.M., Wang, J.L., Xie, S., Qian, C.M.

OCA: Protected "4zdt" [edit=sysop:move=sysop]

OCA — Thu, 30 Apr 2015 10:13:38 GMT

Protected "4zdt" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:13, 30 April 2015

OCA: New page: '''Unreleased structure''' The entry 4zdt is ON HOLD Authors: Lian, F.M., Wang, J.L., Xie, S., Qian, C.M. Description: Crystal structure of the RING finger domain of Slx1 in complex wi...

OCA — Thu, 30 Apr 2015 10:13:37 GMT

New page: '''Unreleased structure''' The entry 4zdt is ON HOLD Authors: Lian, F.M., Wang, J.L., Xie, S., Qian, C.M. Description: Crystal structure of the RING finger domain of Slx1 in complex wi...

New page

'''Unreleased structure'''

The entry 4zdt is ON HOLD

Authors: Lian, F.M., Wang, J.L., Xie, S., Qian, C.M.

Description: Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4
[[Category: Unreleased Structures]]
[[Category: Xie, S]]
[[Category: Wang, J.L]]
[[Category: Lian, F.M]]
[[Category: Qian, C.M]]