5n85 - Revision history

OCA at 12:33, 15 November 2023

OCA — Wed, 15 Nov 2023 12:33:45 GMT

←Older revision		Revision as of 12:33, 15 November 2023
Line 3:		Line 3:
	<StructureSection load='5n85' size='340' side='right'caption='[[5n85]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5n85' size='340' side='right'caption='[[5n85]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5n85]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N85 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5N85 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5n85]] 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=5N85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N85 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5n85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n85 OCA], [~~http~~://pdbe.org/5n85 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5n85 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5n85 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5n85 ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5n85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n85 OCA], [https://pdbe.org/5n85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n85 RCSB], [https://www.ebi.ac.uk/pdbsum/5n85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n85 ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/PRIPO_HUMAN PRIPO_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> [[http://www.uniprot.org/uniprot/PRIPO_HUMAN PRIPO_HUMAN]] DNA primase and DNA polymerase able to initiate de novo DNA synthesis using dNTPs. Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA. Involved in translesion synthesis via its primase activity by mediating uninterrupted fork progression after programmed or damage-induced fork arrest and by reinitiating DNA synthesis after dNTP depletion. Required for mitochondrial DNA (mtDNA) synthesis, suggesting it may be involved in DNA tolerance during the replication of mitochondrial DNA. Has non-overlapping function with POLH.<ref>PMID:24126761</ref> <ref>PMID:24207056</ref> <ref>PMID:24240614</ref> <ref>PMID:24267451</ref>	+	[https://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brissett~~, N C~~]]	+	[[Category: Brissett NC]]
-	[[Category: Doherty~~, A J]]~~	+	[[Category: Doherty AJ]]
-	~~[[Category: Basic cleft]]~~	+
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Replication~~]]	+

OCA at 11:58, 26 August 2020

OCA — Wed, 26 Aug 2020 11:58:45 GMT

←Older revision		Revision as of 11:58, 26 August 2020
Line 1:		Line 1:

	==Structure of RPA70N in complex with PrimPol (fragment 514-525)==		==Structure of RPA70N in complex with PrimPol (fragment 514-525)==
-	<StructureSection load='5n85' size='340' side='right' caption='[[5n85]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5n85' size='340' side='right'caption='[[5n85]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5n85]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N85 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5N85 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5n85]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N85 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5N85 FirstGlance]. <br>
-	</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=5n85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n85 OCA], [http://pdbe.org/5n85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n85 RCSB], [http://www.ebi.ac.uk/pdbsum/5n85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n85 ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5n85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n85 OCA], [http://pdbe.org/5n85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n85 RCSB], [http://www.ebi.ac.uk/pdbsum/5n85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n85 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5n85" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5n85" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Single-stranded DNA-binding protein 3D structures\|Single-stranded DNA-binding protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Brissett, N C]]		[[Category: Brissett, N C]]
	[[Category: Doherty, A J]]		[[Category: Doherty, A J]]

OCA at 04:08, 30 August 2017

OCA — Wed, 30 Aug 2017 04:08:35 GMT

←Older revision		Revision as of 04:08, 30 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5n85 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Structure of RPA70N in complex with PrimPol (fragment 514-525)==
		+	<StructureSection load='5n85' size='340' side='right' caption='[[5n85]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5n85]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N85 FirstGlance]. <br>
		+	</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=5n85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n85 OCA], [http://pdbe.org/5n85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n85 RCSB], [http://www.ebi.ac.uk/pdbsum/5n85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n85 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PRIPO_HUMAN PRIPO_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> [[http://www.uniprot.org/uniprot/PRIPO_HUMAN PRIPO_HUMAN]] DNA primase and DNA polymerase able to initiate de novo DNA synthesis using dNTPs. Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA. Involved in translesion synthesis via its primase activity by mediating uninterrupted fork progression after programmed or damage-induced fork arrest and by reinitiating DNA synthesis after dNTP depletion. Required for mitochondrial DNA (mtDNA) synthesis, suggesting it may be involved in DNA tolerance during the replication of mitochondrial DNA. Has non-overlapping function with POLH.<ref>PMID:24126761</ref> <ref>PMID:24207056</ref> <ref>PMID:24240614</ref> <ref>PMID:24267451</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DNA damage and secondary structures can stall the replication machinery. Cells possess numerous tolerance mechanisms to complete genome duplication in the presence of such impediments. In addition to translesion synthesis (TLS) polymerases, most eukaryotic cells contain a multifunctional replicative enzyme called primase-polymerase (PrimPol) that is capable of directly bypassing DNA damage by TLS, as well as repriming replication downstream of impediments. Here, we report that PrimPol is recruited to reprime through its interaction with RPA. Using biophysical and crystallographic approaches, we identify that PrimPol possesses two RPA-binding motifs and ascertained the key residues required for these interactions. We demonstrate that one of these motifs is critical for PrimPol's recruitment to stalled replication forks in vivo. In addition, biochemical analysis reveals that RPA serves to stimulate the primase activity of PrimPol. Together, these findings provide significant molecular insights into PrimPol's mode of recruitment to stalled forks to facilitate repriming and restart.

-	~~Authors: Brissett, N.C~~., ~~Doherty~~, A.J.	+	Molecular basis for PrimPol recruitment to replication forks by RPA.,Guilliam TA, Brissett NC, Ehlinger A, Keen BA, Kolesar P, Taylor EM, Bailey LJ, Lindsay HD, Chazin WJ, Doherty AJ Nat Commun. 2017 May 23;8:15222. doi: 10.1038/ncomms15222. PMID:28534480<ref>PMID:28534480</ref>

-	~~Description: Structure~~ of ~~RPA70N in complex with PrimPol (fragment 514-525)~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
-	[[Category: Brissett, N.C]]	+	<div class="pdbe-citations 5n85" style="background-color:#fffaf0;"></div>
-	[[Category: Doherty, A.J]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Brissett, N C]]
		+	[[Category: Doherty, A J]]
		+	[[Category: Basic cleft]]
		+	[[Category: Complex]]
		+	[[Category: Protein binding]]
		+	[[Category: Replication]]

OCA at 09:05, 4 May 2017

OCA — Thu, 04 May 2017 09:05:11 GMT

←Older revision		Revision as of 09:05, 4 May 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5n85 is ON HOLD	+	The entry 5n85 is ON HOLD until Paper Publication

	Authors: Brissett, N.C., Doherty, A.J.		Authors: Brissett, N.C., Doherty, A.J.

OCA at 09:46, 5 April 2017

OCA — Wed, 05 Apr 2017 09:46:47 GMT

←Older revision		Revision as of 09:46, 5 April 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5n85 is ON HOLD ~~until sometime in the future~~	+	The entry 5n85 is ON HOLD

	Authors: Brissett, N.C., Doherty, A.J.		Authors: Brissett, N.C., Doherty, A.J.

OCA: Protected "5n85" [edit=sysop:move=sysop]

OCA — Thu, 09 Mar 2017 12:15:02 GMT

Protected "5n85" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:15, 9 March 2017

OCA: New page: '''Unreleased structure''' The entry 5n85 is ON HOLD until sometime in the future Authors: Brissett, N.C., Doherty, A.J. Description: Structure of RPA70N in complex with PrimPol (fragm...

OCA — Thu, 09 Mar 2017 12:15:00 GMT

New page: '''Unreleased structure''' The entry 5n85 is ON HOLD until sometime in the future Authors: Brissett, N.C., Doherty, A.J. Description: Structure of RPA70N in complex with PrimPol (fragm...

New page

'''Unreleased structure'''

The entry 5n85 is ON HOLD until sometime in the future

Authors: Brissett, N.C., Doherty, A.J.

Description: Structure of RPA70N in complex with PrimPol (fragment 514-525)
[[Category: Unreleased Structures]]
[[Category: Brissett, N.C]]
[[Category: Doherty, A.J]]