5mkw - Revision history

OCA at 07:26, 1 May 2024

OCA — Wed, 01 May 2024 07:26:22 GMT

←Older revision		Revision as of 07:26, 1 May 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ZRAB3_HUMAN ZRAB3_HUMAN] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.<ref>PMID:21078962</ref> <ref>PMID:22704558</ref> <ref>PMID:22705370</ref> <ref>PMID:22759634</ref> <ref>PMID:26884333</ref>		[https://www.uniprot.org/uniprot/ZRAB3_HUMAN ZRAB3_HUMAN] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.<ref>PMID:21078962</ref> <ref>PMID:22704558</ref> <ref>PMID:22705370</ref> <ref>PMID:22759634</ref> <ref>PMID:26884333</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Strategies to resolve replication blocks are critical for the maintenance of genome stability. Among the factors implicated in the replication stress response is the ATP-dependent endonuclease ZRANB3. Here, we present the structure of the ZRANB3 HNH (His-Asn-His) endonuclease domain and provide a detailed analysis of its activity. We further define PCNA as a key regulator of ZRANB3 function, which recruits ZRANB3 to stalled replication forks and stimulates its endonuclease activity. Finally, we present the co-crystal structures of PCNA with two specific motifs in ZRANB3: the PIP box and the APIM motif. Our data provide important structural insights into the PCNA-APIM interaction, and reveal unexpected similarities between the PIP box and the APIM motif. We propose that PCNA and ATP-dependency serve as a multi-layered regulatory mechanism that modulates ZRANB3 activity at replication forks. Importantly, our findings allow us to interpret the functional significance of cancer associated ZRANB3 mutations.
-
-	Structural insights into the function of ZRANB3 in replication stress response.,Sebesta M, Cooper CDO, Ariza A, Carnie CJ, Ahel D Nat Commun. 2017 Jun 16;8:15847. doi: 10.1038/ncomms15847. PMID:28621305<ref>PMID:28621305</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5mkw" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:48, 1 November 2023

OCA — Wed, 01 Nov 2023 18:48:58 GMT

←Older revision		Revision as of 18:48, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='5mkw' size='340' side='right'caption='[[5mkw]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5mkw' size='340' side='right'caption='[[5mkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5mkw]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5MKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5mkw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MKW 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=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='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~ZRANB3 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN])~~</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=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=5mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkw OCA], [~~http~~://pdbe.org/5mkw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5mkw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5mkw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkw 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=5mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkw OCA], [https://pdbe.org/5mkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mkw RCSB], [https://www.ebi.ac.uk/pdbsum/5mkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ZRAB3_HUMAN ZRAB3_HUMAN]] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.<ref>PMID:21078962</ref> <ref>PMID:22704558</ref> <ref>PMID:22705370</ref> <ref>PMID:22759634</ref> <ref>PMID:26884333</ref>	+	[https://www.uniprot.org/uniprot/ZRAB3_HUMAN ZRAB3_HUMAN] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.<ref>PMID:21078962</ref> <ref>PMID:22704558</ref> <ref>PMID:22705370</ref> <ref>PMID:22759634</ref> <ref>PMID:26884333</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ariza, A]]	+	[[Category: Ariza A]]
-	~~[[Category: Dna-binding]]~~	+
-	~~[[Category: Endonuclease]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metalloprotein]]~~	+
-	~~[[Category: Zinc-binding~~]]	+

OCA at 05:50, 10 October 2019

OCA — Thu, 10 Oct 2019 05:50:39 GMT

←Older revision		Revision as of 05:50, 10 October 2019
Line 1:		Line 1:

	==Crystal structure of the human ZRANB3 HNH domain==		==Crystal structure of the human ZRANB3 HNH domain==
-	<StructureSection load='5mkw' size='340' side='right' caption='[[5mkw]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5mkw' size='340' side='right'caption='[[5mkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5mkw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MKW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5mkw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MKW 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=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=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ZRANB3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkw OCA], [http://pdbe.org/5mkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mkw RCSB], [http://www.ebi.ac.uk/pdbsum/5mkw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkw 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=5mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkw OCA], [http://pdbe.org/5mkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mkw RCSB], [http://www.ebi.ac.uk/pdbsum/5mkw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkw ProSAT]</span></td></tr>
	</table>		</table>
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ariza, A]]		[[Category: Ariza, A]]
	[[Category: Dna-binding]]		[[Category: Dna-binding]]

OCA at 04:14, 30 August 2017

OCA — Wed, 30 Aug 2017 04:14:38 GMT

←Older revision		Revision as of 04:14, 30 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5mkw is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of the human ZRANB3 HNH domain==
		+	<StructureSection load='5mkw' size='340' side='right' caption='[[5mkw]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5mkw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MKW 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=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=5mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkw OCA], [http://pdbe.org/5mkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mkw RCSB], [http://www.ebi.ac.uk/pdbsum/5mkw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkw ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ZRAB3_HUMAN ZRAB3_HUMAN]] DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.<ref>PMID:21078962</ref> <ref>PMID:22704558</ref> <ref>PMID:22705370</ref> <ref>PMID:22759634</ref> <ref>PMID:26884333</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Strategies to resolve replication blocks are critical for the maintenance of genome stability. Among the factors implicated in the replication stress response is the ATP-dependent endonuclease ZRANB3. Here, we present the structure of the ZRANB3 HNH (His-Asn-His) endonuclease domain and provide a detailed analysis of its activity. We further define PCNA as a key regulator of ZRANB3 function, which recruits ZRANB3 to stalled replication forks and stimulates its endonuclease activity. Finally, we present the co-crystal structures of PCNA with two specific motifs in ZRANB3: the PIP box and the APIM motif. Our data provide important structural insights into the PCNA-APIM interaction, and reveal unexpected similarities between the PIP box and the APIM motif. We propose that PCNA and ATP-dependency serve as a multi-layered regulatory mechanism that modulates ZRANB3 activity at replication forks. Importantly, our findings allow us to interpret the functional significance of cancer associated ZRANB3 mutations.

-	~~Authors~~:	+	Structural insights into the function of ZRANB3 in replication stress response.,Sebesta M, Cooper CDO, Ariza A, Carnie CJ, Ahel D Nat Commun. 2017 Jun 16;8:15847. doi: 10.1038/ncomms15847. PMID:28621305<ref>PMID:28621305</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5mkw" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ariza, A]]
		+	[[Category: Dna-binding]]
		+	[[Category: Endonuclease]]
		+	[[Category: Hydrolase]]
		+	[[Category: Metalloprotein]]
		+	[[Category: Zinc-binding]]

OCA: Protected "5mkw" [edit=sysop:move=sysop]

OCA — Thu, 15 Dec 2016 16:25:59 GMT

Protected "5mkw" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:25, 15 December 2016

OCA: New page: '''Unreleased structure''' The entry 5mkw is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Thu, 15 Dec 2016 16:25:57 GMT

New page: '''Unreleased structure''' The entry 5mkw is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5mkw is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]