4cgy - Revision history

OCA at 12:10, 20 December 2023

OCA — Wed, 20 Dec 2023 12:10:08 GMT

←Older revision		Revision as of 12:10, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cgy]] 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=4CGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CGY FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cgy]] 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=4CGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CGY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.85Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [https://pdbe.org/4cgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [https://www.ebi.ac.uk/pdbsum/4cgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgy 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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [https://pdbe.org/4cgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [https://www.ebi.ac.uk/pdbsum/4cgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TOP3A_HUMAN TOP3A_HUMAN]] Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity.<ref>PMID:8622991</ref> <ref>PMID:20445207</ref>	+	[https://www.uniprot.org/uniprot/TOP3A_HUMAN TOP3A_HUMAN] Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity.<ref>PMID:8622991</ref> <ref>PMID:20445207</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Repair of DNA double-strand breaks via homologous recombination can produce double Holliday junctions (dHJs) that require enzymatic separation. Topoisomerase IIIalpha (TopIIIalpha) together with RMI1 disentangles the final hemicatenane intermediate obtained once dHJs have converged. How binding of RMI1 to TopIIIalpha influences it to behave as a hemicatenane dissolvase, rather than as an enzyme that relaxes DNA topology, is unknown. Here, we present the crystal structure of human TopIIIalpha complexed to the first oligonucleotide-binding domain (OB fold) of RMI1. TopIII assumes a toroidal type 1A topoisomerase fold. RMI1 attaches to the edge of the gate in TopIIIalpha through which DNA passes. RMI1 projects a 23-residue loop into the TopIIIalpha gate, thereby influencing the dynamics of its opening and closing. Our results provide a mechanistic rationale for how RMI1 stabilizes TopIIIalpha-gate opening to enable dissolution and illustrate how binding partners modulate topoisomerase function.
		+
		+	Structural and mechanistic insight into Holliday-junction dissolution by Topoisomerase IIIalpha and RMI1.,Bocquet N, Bizard AH, Abdulrahman W, Larsen NB, Faty M, Cavadini S, Bunker RD, Kowalczykowski SC, Cejka P, Hickson ID, Thoma NH Nat Struct Mol Biol. 2014 Feb 9. doi: 10.1038/nsmb.2775. PMID:24509834<ref>PMID:24509834</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4cgy" style="background-color:#fffaf0;"></div>

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

OCA at 17:45, 7 September 2022

OCA — Wed, 07 Sep 2022 17:45:41 GMT

←Older revision		Revision as of 17:45, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4cgy' size='340' side='right'caption='[[4cgy]], [[Resolution\|resolution]] 2.85Å' scene=''>		<StructureSection load='4cgy' size='340' side='right'caption='[[4cgy]], [[Resolution\|resolution]] 2.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cgy]] 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=4CGY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CGY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cgy]] 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=4CGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CGY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] </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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [https://pdbe.org/4cgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [https://www.ebi.ac.uk/pdbsum/4cgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgy 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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [~~http~~://pdbe.org/4cgy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cgy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgy ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TOP3A_HUMAN TOP3A_HUMAN]] Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity.<ref>PMID:8622991</ref> <ref>PMID:20445207</ref> [[http://www.uniprot.org/uniprot/RMI1_HUMAN RMI1_HUMAN]] Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.<ref>PMID:15775963</ref> <ref>PMID:16595695</ref> <ref>PMID:16537486</ref>	+	[[https://www.uniprot.org/uniprot/TOP3A_HUMAN TOP3A_HUMAN]] Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity.<ref>PMID:8622991</ref> <ref>PMID:20445207</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Repair of DNA double-strand breaks via homologous recombination can produce double Holliday junctions (dHJs) that require enzymatic separation. Topoisomerase IIIalpha (TopIIIalpha) together with RMI1 disentangles the final hemicatenane intermediate obtained once dHJs have converged. How binding of RMI1 to TopIIIalpha influences it to behave as a hemicatenane dissolvase, rather than as an enzyme that relaxes DNA topology, is unknown. Here, we present the crystal structure of human TopIIIalpha complexed to the first oligonucleotide-binding domain (OB fold) of RMI1. TopIII assumes a toroidal type 1A topoisomerase fold. RMI1 attaches to the edge of the gate in TopIIIalpha through which DNA passes. RMI1 projects a 23-residue loop into the TopIIIalpha gate, thereby influencing the dynamics of its opening and closing. Our results provide a mechanistic rationale for how RMI1 stabilizes TopIIIalpha-gate opening to enable dissolution and illustrate how binding partners modulate topoisomerase function.	+
-		+
-	Structural and mechanistic insight into Holliday-junction dissolution by Topoisomerase IIIalpha and RMI1.,Bocquet N, Bizard AH, Abdulrahman W, Larsen NB, Faty M, Cavadini S, Bunker RD, Kowalczykowski SC, Cejka P, Hickson ID, Thoma NH Nat Struct Mol Biol. 2014 Feb 9. doi: 10.1038/nsmb.2775. PMID:24509834<ref>PMID:24509834</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4cgy" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
-	*[[Topoisomerase\|Topoisomerase]]	+	*[[Topoisomerase 3D structures\|Topoisomerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~DNA topoisomerase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bocquet, N]]	+	[[Category: Bocquet N]]
-	[[Category: Bunker~~, R D~~]]	+	[[Category: Bunker RD]]
-	[[Category: Thoma~~, N H]]~~	+	[[Category: Thoma NH]]
-	~~[[Category: Decatenation]]~~	+
-	~~[[Category: Dna replication-isomerase complex]]~~	+
-	~~[[Category: Double holliday junction dissolution]]~~	+
-	~~[[Category: Minimal dissolvasome~~]]	+

OCA at 09:11, 20 March 2019

OCA — Wed, 20 Mar 2019 09:11:20 GMT

←Older revision		Revision as of 09:11, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of the human topoisomerase III alpha-RMI1 complex==		==Crystal structure of the human topoisomerase III alpha-RMI1 complex==
-	<StructureSection load='4cgy' size='340' side='right' caption='[[4cgy]], [[Resolution\|resolution]] 2.85Å' scene=''>	+	<StructureSection load='4cgy' size='340' side='right'caption='[[4cgy]], [[Resolution\|resolution]] 2.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cgy]] 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=4CGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CGY FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cgy]] 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=4CGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CGY FirstGlance]. <br>
Line 28:		Line 28:
	[[Category: DNA topoisomerase]]		[[Category: DNA topoisomerase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bocquet, N]]		[[Category: Bocquet, N]]
	[[Category: Bunker, R D]]		[[Category: Bunker, R D]]

OCA at 13:45, 4 August 2016

OCA — Thu, 04 Aug 2016 13:45:12 GMT

←Older revision		Revision as of 13:45, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the human topoisomerase III alpha-RMI1 complex==		==Crystal structure of the human topoisomerase III alpha-RMI1 complex==
	<StructureSection load='4cgy' size='340' side='right' caption='[[4cgy]], [[Resolution\|resolution]] 2.85Å' scene=''>		<StructureSection load='4cgy' size='340' side='right' caption='[[4cgy]], [[Resolution\|resolution]] 2.85Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] </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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [http://www.ebi.ac.uk/pdbsum/4cgy PDBsum]</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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [http://pdbe.org/4cgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [http://www.ebi.ac.uk/pdbsum/4cgy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4cgy" style="background-color:#fffaf0;"></div>

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

OCA at 15:14, 24 December 2014

OCA — Wed, 24 Dec 2014 15:14:04 GMT

←Older revision		Revision as of 15:14, 24 December 2014
Line 7:		Line 7:
	<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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [http://www.ebi.ac.uk/pdbsum/4cgy PDBsum]</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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [http://www.ebi.ac.uk/pdbsum/4cgy PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TOP3A_HUMAN TOP3A_HUMAN]] Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity.<ref>PMID:8622991</ref> <ref>PMID:20445207</ref> [[http://www.uniprot.org/uniprot/RMI1_HUMAN RMI1_HUMAN]] Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.<ref>PMID:15775963</ref> <ref>PMID:16595695</ref> <ref>PMID:16537486</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:11, 21 December 2014

OCA — Sun, 21 Dec 2014 18:11:41 GMT

←Older revision		Revision as of 18:11, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4cgy\| PDB=4cgy \| SCENE= }}~~	+	==Crystal structure of the human topoisomerase III alpha-RMI1 complex==
-	===Crystal structure of the human topoisomerase III alpha-RMI1 complex===	+	<StructureSection load='4cgy' size='340' side='right' caption='[[4cgy]], [[Resolution\|resolution]] 2.85Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24509834}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4cgy]] 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=4CGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CGY FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_topoisomerase DNA topoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.2 5.99.1.2] </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=4cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgy RCSB], [http://www.ebi.ac.uk/pdbsum/4cgy PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Repair of DNA double-strand breaks via homologous recombination can produce double Holliday junctions (dHJs) that require enzymatic separation. Topoisomerase IIIalpha (TopIIIalpha) together with RMI1 disentangles the final hemicatenane intermediate obtained once dHJs have converged. How binding of RMI1 to TopIIIalpha influences it to behave as a hemicatenane dissolvase, rather than as an enzyme that relaxes DNA topology, is unknown. Here, we present the crystal structure of human TopIIIalpha complexed to the first oligonucleotide-binding domain (OB fold) of RMI1. TopIII assumes a toroidal type 1A topoisomerase fold. RMI1 attaches to the edge of the gate in TopIIIalpha through which DNA passes. RMI1 projects a 23-residue loop into the TopIIIalpha gate, thereby influencing the dynamics of its opening and closing. Our results provide a mechanistic rationale for how RMI1 stabilizes TopIIIalpha-gate opening to enable dissolution and illustrate how binding partners modulate topoisomerase function.

-	~~==Function==~~	+	Structural and mechanistic insight into Holliday-junction dissolution by Topoisomerase IIIalpha and RMI1.,Bocquet N, Bizard AH, Abdulrahman W, Larsen NB, Faty M, Cavadini S, Bunker RD, Kowalczykowski SC, Cejka P, Hickson ID, Thoma NH Nat Struct Mol Biol. 2014 Feb 9. doi: 10.1038/nsmb.2775. PMID:24509834<ref>PMID:24509834</ref>
-	~~[[http://www.uniprot.org/uniprot/TOP3A_HUMAN TOP3A_HUMAN]] Releases the supercoiling~~ and ~~torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single~~-~~strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked~~ by ~~the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate~~ and ~~the expulsion of a 3'-OH DNA strand~~. ~~The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally~~, ~~in the religation step~~, ~~the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex~~, ~~a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells~~. ~~Has DNA decatenation activity~~.~~<ref>PMID~~:~~8622991</ref> <ref>PMID:20445207</ref> [[http://www~~.~~uniprot.org~~/uniprot/RMI1_HUMAN RMI1_HUMAN]] Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. ~~Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution~~. ~~Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.<ref>~~PMID:~~15775963</ref> <ref>PMID:16595695</ref>~~ <ref>PMID:~~16537486~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4cgy]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4CGY OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:024509834</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Topoisomerase\|Topoisomerase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: DNA topoisomerase]]		[[Category: DNA topoisomerase]]
-	[[Category: Bocquet, N.]]	+	[[Category: Human]]
-	[[Category: Bunker, R D.]]	+	[[Category: Bocquet, N]]
-	[[Category: Thoma, N H.]]	+	[[Category: Bunker, R D]]
		+	[[Category: Thoma, N H]]
	[[Category: Decatenation]]		[[Category: Decatenation]]
	[[Category: Dna replication-isomerase complex]]		[[Category: Dna replication-isomerase complex]]
	[[Category: Double holliday junction dissolution]]		[[Category: Double holliday junction dissolution]]
	[[Category: Minimal dissolvasome]]		[[Category: Minimal dissolvasome]]

OCA at 14:59, 19 February 2014

OCA — Wed, 19 Feb 2014 14:59:02 GMT

←Older revision		Revision as of 14:59, 19 February 2014
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	{{STRUCTURE_4cgy\| PDB=4cgy \| SCENE= }}		{{STRUCTURE_4cgy\| PDB=4cgy \| SCENE= }}
	===Crystal structure of the human topoisomerase III alpha-RMI1 complex===		===Crystal structure of the human topoisomerase III alpha-RMI1 complex===
		+	{{ABSTRACT_PUBMED_24509834}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024509834</ref><references group="xtra"/><references/>
	[[Category: DNA topoisomerase]]		[[Category: DNA topoisomerase]]
	[[Category: Bocquet, N.]]		[[Category: Bocquet, N.]]

OCA at 05:15, 13 February 2014

OCA — Thu, 13 Feb 2014 05:15:30 GMT

←Older revision		Revision as of 05:15, 13 February 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4cgy\| PDB=4cgy \| SCENE= }}
		+	===Crystal structure of the human topoisomerase III alpha-RMI1 complex===

-	The ~~entry 4cgy~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/TOP3A_HUMAN TOP3A_HUMAN]] Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity.<ref>PMID:8622991</ref> <ref>PMID:20445207</ref> [[http://www.uniprot.org/uniprot/RMI1_HUMAN RMI1_HUMAN]] Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.<ref>PMID:15775963</ref> <ref>PMID:16595695</ref> <ref>PMID:16537486</ref>

-	~~Authors: Bocquet, N~~.~~, Bunker, R~~.D.~~, Thoma, N~~.H.	+	==About this Structure==
		+	[[4cgy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CGY OCA].

-	~~Description~~: ~~Crystal structure of the human~~ topoisomerase ~~III alpha~~-~~RMI1~~ complex	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: DNA topoisomerase]]
		+	[[Category: Bocquet, N.]]
		+	[[Category: Bunker, R D.]]
		+	[[Category: Thoma, N H.]]
		+	[[Category: Decatenation]]
		+	[[Category: Dna replication-isomerase complex]]
		+	[[Category: Double holliday junction dissolution]]
		+	[[Category: Minimal dissolvasome]]

OCA at 12:47, 11 December 2013

OCA — Wed, 11 Dec 2013 12:47:10 GMT

←Older revision		Revision as of 12:47, 11 December 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Bocquet, N., Bunker, R.D., Thoma, N.H.		Authors: Bocquet, N., Bunker, R.D., Thoma, N.H.

	Description: Crystal structure of the human topoisomerase III alpha-RMI1 complex		Description: Crystal structure of the human topoisomerase III alpha-RMI1 complex

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

OCA — Wed, 04 Dec 2013 06:32:04 GMT

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

←Older revision

Revision as of 06:32, 4 December 2013