5zoe - Revision history

OCA at 09:02, 22 November 2023

OCA — Wed, 22 Nov 2023 09:02:03 GMT

←Older revision		Revision as of 09:02, 22 November 2023
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	<StructureSection load='5zoe' size='340' side='right'caption='[[5zoe]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='5zoe' size='340' side='right'caption='[[5zoe]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zoe]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5ZOE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zoe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZOE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 1.95Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5um9\|5um9]]~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=5zoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoe OCA], [~~http~~://pdbe.org/5zoe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zoe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zoe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoe 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=5zoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoe OCA], [https://pdbe.org/5zoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zoe RCSB], [https://www.ebi.ac.uk/pdbsum/5zoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FEN1_HUMAN FEN1_HUMAN]] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.<ref>PMID:7961795</ref> <ref>PMID:8621570</ref> <ref>PMID:10744741</ref> <ref>PMID:11986308</ref> <ref>PMID:18443037</ref> <ref>PMID:20729856</ref>	+	[https://www.uniprot.org/uniprot/FEN1_HUMAN FEN1_HUMAN] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.<ref>PMID:7961795</ref> <ref>PMID:8621570</ref> <ref>PMID:10744741</ref> <ref>PMID:11986308</ref> <ref>PMID:18443037</ref> <ref>PMID:20729856</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Han, W~~]]	+	[[Category: Synthetic construct]]
-	[[Category: ~~Hua, Y~~]]	+	[[Category: Han W]]
-	[[Category: ~~Zhao,~~ Y]]	+	[[Category: Hua Y]]
-	[[Category: ~~Dna binding protein]]~~	+	[[Category: Zhao Y]]
-	~~[[Category: Flap endonuclease: gap endonuclease: methylation: posttranslational modification]]~~	+
-	~~[[Category: Hydrolase-dna complex~~]]	+

OCA at 08:29, 4 November 2020

OCA — Wed, 04 Nov 2020 08:29:35 GMT

←Older revision		Revision as of 08:29, 4 November 2020
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	==Crystal Structure of D181A hFen1 in complex with DNA==		==Crystal Structure of D181A hFen1 in complex with DNA==
-	<StructureSection load='5zoe' size='340' side='right' caption='[[5zoe]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='5zoe' size='340' side='right'caption='[[5zoe]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zoe]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZOE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zoe]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZOE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5um9\|5um9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5um9\|5um9]]</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=5zoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoe OCA], [http://pdbe.org/5zoe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zoe RCSB], [http://www.ebi.ac.uk/pdbsum/5zoe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoe ProSAT]</span></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=5zoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoe OCA], [http://pdbe.org/5zoe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zoe RCSB], [http://www.ebi.ac.uk/pdbsum/5zoe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 5zoe" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5zoe" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Endonuclease 3D structures\|Endonuclease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Han, W]]		[[Category: Han, W]]
	[[Category: Hua, Y]]		[[Category: Hua, Y]]

OCA at 08:10, 30 January 2019

OCA — Wed, 30 Jan 2019 08:10:57 GMT

←Older revision		Revision as of 08:10, 30 January 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 5zoe is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal Structure of D181A hFen1 in complex with DNA==
		+	<StructureSection load='5zoe' size='340' side='right' caption='[[5zoe]], [[Resolution\|resolution]] 1.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5zoe]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZOE FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5um9\|5um9]]</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=5zoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoe OCA], [http://pdbe.org/5zoe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zoe RCSB], [http://www.ebi.ac.uk/pdbsum/5zoe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoe ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FEN1_HUMAN FEN1_HUMAN]] Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.<ref>PMID:7961795</ref> <ref>PMID:8621570</ref> <ref>PMID:10744741</ref> <ref>PMID:11986308</ref> <ref>PMID:18443037</ref> <ref>PMID:20729856</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human flap endonuclease 1 (hFEN1) is a structure-specific nuclease essential for DNA replication and repair processes. hFEN1 has 5' flap removal activity, as well as gap endonuclease activity that is critical for restarting stalled replication forks. Here, we report the crystal structures of wild-type and mutant hFEN1 proteins in complex with DNA substrates, followed by mutagenesis studies that provide mechanistic insight into the protein-protein interactions of hFEN1. We found that in an alpha-helix forming the helical gateway of hFEN1 recognizes the 5' flap prior to its threading into the active site for cleavage. We also found that the beta-pin region is rigidified into a short helix in R192F hFEN1-DNA structures, suppressing its gap endonuclease activity and cycle-dependent kinase interactions. Our findings suggest that a single mutation at the primary methylation site can alter the function of hFEN1 and provide insight into the role of the beta-pin region in hFEN1 protein interactions that are essential for DNA replication and repair.

-	~~Authors~~:	+	Structural basis of 5' flap recognition and protein-protein interactions of human flap endonuclease 1.,Xu H, Shi R, Han W, Cheng J, Xu X, Cheng K, Wang L, Tian B, Zheng L, Shen B, Hua Y, Zhao Y Nucleic Acids Res. 2018 Nov 30;46(21):11315-11325. doi: 10.1093/nar/gky911. PMID:30295841<ref>PMID:30295841</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5zoe" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Han, W]]
		+	[[Category: Hua, Y]]
		+	[[Category: Zhao, Y]]
		+	[[Category: Dna binding protein]]
		+	[[Category: Flap endonuclease: gap endonuclease: methylation: posttranslational modification]]
		+	[[Category: Hydrolase-dna complex]]

OCA at 04:43, 9 May 2018

OCA — Wed, 09 May 2018 04:43:14 GMT

←Older revision		Revision as of 04:43, 9 May 2018
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 18 Apr 2018 04:07:50 GMT

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

←Older revision

Revision as of 04:07, 18 April 2018

OCA: New page: '''Unreleased structure''' The entry 5zoe is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 18 Apr 2018 04:07:49 GMT

New page: '''Unreleased structure''' The entry 5zoe is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5zoe is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]