4cht - Revision history

OCA at 12:10, 20 December 2023

2023-12-20T12:10:29Z

← Older revision		Revision as of 12:10, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cht]] 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=4CHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cht]] 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=4CHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 3.25Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [https://pdbe.org/4cht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [https://www.ebi.ac.uk/pdbsum/4cht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cht 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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [https://pdbe.org/4cht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [https://www.ebi.ac.uk/pdbsum/4cht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cht 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 4cht" style="background-color:#fffaf0;"></div>

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

OCA at 17:46, 7 September 2022

2022-09-07T17:46:37Z

← Older revision		Revision as of 17:46, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4cht' size='340' side='right'caption='[[4cht]], [[Resolution\|resolution]] 3.25Å' scene=''>		<StructureSection load='4cht' size='340' side='right'caption='[[4cht]], [[Resolution\|resolution]] 3.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cht]] 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=4CHT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cht]] 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=4CHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cgy\|4cgy]]</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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [https://pdbe.org/4cht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [https://www.ebi.ac.uk/pdbsum/4cht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cht ProSAT]</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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [~~http~~://pdbe.org/4cht PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cht PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cht 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 4cht" 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: Cell cycle]]~~
	~~[[Category: Decatenation]]~~
	~~[[Category: Double holliday junction dissolution]]~~
	~~[[Category: Minimal dissolvasome~~]]

OCA at 09:56, 20 March 2019

2019-03-20T09:56:22Z

← Older revision		Revision as of 09:56, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion==		==Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion==
	<StructureSection load='4cht' size='340' side='right' caption='[[4cht]], [[Resolution\|resolution]] 3.25Å' scene=''>		<StructureSection load='4cht' size='340' side='right'caption='[[4cht]], [[Resolution\|resolution]] 3.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cht]] 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=4CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cht]] 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=4CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHT FirstGlance]. <br>
Line 29:		Line 29:
	[[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 06:26, 5 August 2016

2016-08-05T06:26:48Z

← Older revision		Revision as of 06:26, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion==		==Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion==
	<StructureSection load='4cht' size='340' side='right' caption='[[4cht]], [[Resolution\|resolution]] 3.25Å' scene=''>		<StructureSection load='4cht' size='340' side='right' caption='[[4cht]], [[Resolution\|resolution]] 3.25Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cgy\|4cgy]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cgy\|4cgy]]</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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [http://www.ebi.ac.uk/pdbsum/4cht 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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [http://pdbe.org/4cht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [http://www.ebi.ac.uk/pdbsum/4cht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cht ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4cht" style="background-color:#fffaf0;"></div>

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

OCA at 16:30, 25 December 2014

2014-12-25T16:30:49Z

← Older revision		Revision as of 16:30, 25 December 2014
Line 8:		Line 8:
	<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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [http://www.ebi.ac.uk/pdbsum/4cht 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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [http://www.ebi.ac.uk/pdbsum/4cht 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 17:36, 21 December 2014

2014-12-21T17:36:10Z

← Older revision		Revision as of 17:36, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4cht\| PDB=4cht \| SCENE= }}~~		==Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion==
	===Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion===		<StructureSection load='4cht' size='340' side='right' caption='[[4cht]], [[Resolution\|resolution]] 3.25Å' scene=''>
	~~{{ABSTRACT_PUBMED_24509834}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4cht]] 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=4CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHT FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cgy\|4cgy]]</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=4cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cht RCSB], [http://www.ebi.ac.uk/pdbsum/4cht 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>
	~~[[4cht]] is~~ a ~~2 chain structure. Full crystallographic information is available from [http://oca~~.~~weizmann~~.ac.~~il/oca-bin~~/~~ocashort?id=4CHT 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: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Decatenation]]		[[Category: Decatenation]]
	[[Category: Double holliday junction dissolution]]		[[Category: Double holliday junction dissolution]]
	[[Category: Minimal dissolvasome]]		[[Category: Minimal dissolvasome]]

OCA at 15:16, 19 February 2014

2014-02-19T15:16:22Z

← Older revision		Revision as of 15:16, 19 February 2014
Line 1:		Line 1:
	{{STRUCTURE_4cht\| PDB=4cht \| SCENE= }}		{{STRUCTURE_4cht\| PDB=4cht \| SCENE= }}
	===Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion===		===Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion===
			{{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

2014-02-13T05:15:40Z

← Older revision		Revision as of 05:15, 13 February 2014
Line 1:		Line 1:
	~~'''Unreleased~~ structure~~'''~~		{{STRUCTURE_4cht\| PDB=4cht \| SCENE= }}
			===Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion===

	The ~~entry 4cht~~ is ~~ON HOLD~~		==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==
			[[4cht]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHT OCA].

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

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

2013-12-11T12:47:55Z

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

← Older revision	Revision as of 12:47, 11 December 2013
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4cht is ON HOLD Authors: Bocquet, N., Bunker, R.D., Thoma, N.H. Description: Crystal structure of the human topoisomerase III alpha-RMI1 complex wi...

2013-12-11T12:47:55Z

New page: '''Unreleased structure''' The entry 4cht is ON HOLD Authors: Bocquet, N., Bunker, R.D., Thoma, N.H. Description: Crystal structure of the human topoisomerase III alpha-RMI1 complex wi...

New page

'''Unreleased structure'''

The entry 4cht is ON HOLD

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

Description: Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion