4nck - Revision history

OCA at 12:32, 1 March 2024

OCA — Fri, 01 Mar 2024 12:32:46 GMT

←Older revision		Revision as of 12:32, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4nck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NCK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4nck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NCK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.99Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [https://pdbe.org/4nck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [https://www.ebi.ac.uk/pdbsum/4nck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nck 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=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [https://pdbe.org/4nck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [https://www.ebi.ac.uk/pdbsum/4nck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nck ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]		[https://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The Mre11-Rad50 complex is highly conserved, yet the mechanisms by which Rad50 ATP-driven states regulate the sensing, processing and signaling of DNA double-strand breaks are largely unknown. Here we design structure-based mutations in Pyrococcus furiosus Rad50 to alter protein core plasticity and residues undergoing ATP-driven movements within the catalytic domains. With this strategy we identify Rad50 separation-of-function mutants that either promote or destabilize the ATP-bound state. Crystal structures, X-ray scattering, biochemical assays, and functional analyses of mutant PfRad50 complexes show that the ATP-induced 'closed' conformation promotes DNA end binding and end tethering, while hydrolysis-induced opening is essential for DNA resection. Reducing the stability of the ATP-bound state impairs DNA repair and Tel1 (ATM) checkpoint signaling in Schizosaccharomyces pombe, double-strand break resection in Saccharomyces cerevisiae, and ATM activation by human Mre11-Rad50-Nbs1 in vitro, supporting the generality of the P. furiosus Rad50 structure-based mutational analyses. These collective results suggest that ATP-dependent Rad50 conformations switch the Mre11-Rad50 complex between DNA tethering, ATM signaling, and 5' strand resection, revealing molecular mechanisms regulating responses to DNA double-strand breaks.
-
-	ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling.,Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT EMBO J. 2014 Mar 3;33(5):482-500. doi: 10.1002/embj.201386100. Epub 2014 Feb 3. PMID:24493214<ref>PMID:24493214</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4nck" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[ATPase 3D structures\|ATPase 3D structures]]		*[[ATPase 3D structures\|ATPase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:22, 11 January 2023

OCA — Wed, 11 Jan 2023 08:22:10 GMT

←Older revision		Revision as of 08:22, 11 January 2023
Line 1:		Line 1:

	==Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation==		==Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation==
-	<StructureSection load='4nck' size='340' side='right' caption='[[4nck]], [[Resolution\|resolution]] 1.99Å' scene=''>	+	<StructureSection load='4nck' size='340' side='right'caption='[[4nck]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nck]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pyrfu Pyrfu~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NCK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NCK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nch\|4nch]], [[4nci\|4nci]], [[4ncj\|4ncj]]</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=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [https://pdbe.org/4nck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [https://www.ebi.ac.uk/pdbsum/4nck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nck ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF1167, rad50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])~~</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=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [~~http~~://pdbe.org/4nck PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4nck PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4nck ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]	+	[https://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4nck" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4nck" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATPase 3D structures\|ATPase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Pyrfu~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Arvai, A S~~]]	+	[[Category: Pyrococcus furiosus DSM 3638]]
-	[[Category: ~~Classen, S~~]]	+	[[Category: Arvai AS]]
-	[[Category: ~~Williams, G J~~]]	+	[[Category: Classen S]]
-	[[Category: Williams~~, R S~~]]	+	[[Category: Williams GJ]]
-	[[Category: ~~Adenosine triphosphatase]]~~	+	[[Category: Williams RS]]
-	~~[[Category: Dna binding protein]]~~	+
-	~~[[Category: Dna repair]]~~	+
-	~~[[Category: Fungal protein~~]]	+

OCA at 02:51, 16 November 2017

OCA — Thu, 16 Nov 2017 02:51:26 GMT

←Older revision		Revision as of 02:51, 16 November 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4nck" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4nck" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[ATPase\|ATPase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:55, 4 August 2016

OCA — Thu, 04 Aug 2016 18:55:28 GMT

←Older revision		Revision as of 18:55, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation==		==Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation==
	<StructureSection load='4nck' size='340' side='right' caption='[[4nck]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='4nck' size='340' side='right' caption='[[4nck]], [[Resolution\|resolution]] 1.99Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nch\|4nch]], [[4nci\|4nci]], [[4ncj\|4ncj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nch\|4nch]], [[4nci\|4nci]], [[4ncj\|4ncj]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF1167, rad50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF1167, rad50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [http://www.ebi.ac.uk/pdbsum/4nck 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=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [http://pdbe.org/4nck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [http://www.ebi.ac.uk/pdbsum/4nck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nck 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 4nck" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATPase\|ATPase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:09, 25 December 2014

OCA — Thu, 25 Dec 2014 12:09:31 GMT

←Older revision		Revision as of 12:09, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4nck]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NCK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4nck]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NCK FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nch\|4nch]], [[4nci\|4nci]], [[4ncj\|4ncj]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nch\|4nch]], [[4nci\|4nci]], [[4ncj\|4ncj]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF1167, rad50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF1167, rad50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [http://www.ebi.ac.uk/pdbsum/4nck 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=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [http://www.ebi.ac.uk/pdbsum/4nck PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 16:
	ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling.,Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT EMBO J. 2014 Mar 3;33(5):482-500. doi: 10.1002/embj.201386100. Epub 2014 Feb 3. PMID:24493214<ref>PMID:24493214</ref>		ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling.,Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT EMBO J. 2014 Mar 3;33(5):482-500. doi: 10.1002/embj.201386100. Epub 2014 Feb 3. PMID:24493214<ref>PMID:24493214</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Pyrfu]]		[[Category: Pyrfu]]
-	[[Category: Arvai, A S.]]	+	[[Category: Arvai, A S]]
-	[[Category: Classen, S.]]	+	[[Category: Classen, S]]
-	[[Category: Williams, G J.]]	+	[[Category: Williams, G J]]
-	[[Category: Williams, R S.]]	+	[[Category: Williams, R S]]
	[[Category: Adenosine triphosphatase]]		[[Category: Adenosine triphosphatase]]
	[[Category: Dna binding protein]]		[[Category: Dna binding protein]]
	[[Category: Dna repair]]		[[Category: Dna repair]]
	[[Category: Fungal protein]]		[[Category: Fungal protein]]

OCA at 12:25, 18 May 2014

OCA — Sun, 18 May 2014 12:25:03 GMT

←Older revision		Revision as of 12:25, 18 May 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4nck\| PDB=4nck \| SCENE= }}~~	+	==Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation==
-	===Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation===	+	<StructureSection load='4nck' size='340' side='right' caption='[[4nck]], [[Resolution\|resolution]] 1.99Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24493214}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4nck]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NCK FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4nch\|4nch]], [[4nci\|4nci]], [[4ncj\|4ncj]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PF1167, rad50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nck RCSB], [http://www.ebi.ac.uk/pdbsum/4nck PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Mre11-Rad50 complex is highly conserved, yet the mechanisms by which Rad50 ATP-driven states regulate the sensing, processing and signaling of DNA double-strand breaks are largely unknown. Here we design structure-based mutations in Pyrococcus furiosus Rad50 to alter protein core plasticity and residues undergoing ATP-driven movements within the catalytic domains. With this strategy we identify Rad50 separation-of-function mutants that either promote or destabilize the ATP-bound state. Crystal structures, X-ray scattering, biochemical assays, and functional analyses of mutant PfRad50 complexes show that the ATP-induced 'closed' conformation promotes DNA end binding and end tethering, while hydrolysis-induced opening is essential for DNA resection. Reducing the stability of the ATP-bound state impairs DNA repair and Tel1 (ATM) checkpoint signaling in Schizosaccharomyces pombe, double-strand break resection in Saccharomyces cerevisiae, and ATM activation by human Mre11-Rad50-Nbs1 in vitro, supporting the generality of the P. furiosus Rad50 structure-based mutational analyses. These collective results suggest that ATP-dependent Rad50 conformations switch the Mre11-Rad50 complex between DNA tethering, ATM signaling, and 5' strand resection, revealing molecular mechanisms regulating responses to DNA double-strand breaks.

-	~~==Function==~~	+	ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling.,Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT EMBO J. 2014 Mar 3;33(5):482-500. doi: 10.1002/embj.201386100. Epub 2014 Feb 3. PMID:24493214<ref>PMID:24493214</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/RAD50_PYRFU RAD50_PYRFU]] Involved in DNA double-strand break repair~~ (~~DSBR~~). ~~The Rad50~~/~~Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific~~ 3~~'-5' exonuclease activity~~. ~~Rad50 provides an ATP-dependent control of Mre11 by unwinding and~~/~~or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]~~	+

-	~~==About this Structure==~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4nck]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4NCK OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024493214</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
		+	[[Category: Pyrfu]]
	[[Category: Arvai, A S.]]		[[Category: Arvai, A S.]]
	[[Category: Classen, S.]]		[[Category: Classen, S.]]

OCA at 07:37, 2 April 2014

OCA — Wed, 02 Apr 2014 07:37:21 GMT

←Older revision		Revision as of 07:37, 2 April 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4nck\| PDB=4nck \| SCENE= }}
		+	===Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation===
		+	{{ABSTRACT_PUBMED_24493214}}

-	The ~~entry 4nck is ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]

-	~~Authors~~: ~~Classen, S., Williams, G.J., Arvai, A~~.S.~~, Williams, R~~.S.	+	==About this Structure==
		+	[[4nck]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NCK OCA].

-	~~Description~~: ~~Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation~~	+	==Reference==
		+	<ref group="xtra">PMID:024493214</ref><references group="xtra"/><references/>
		+	[[Category: Arvai, A S.]]
		+	[[Category: Classen, S.]]
		+	[[Category: Williams, G J.]]
		+	[[Category: Williams, R S.]]
		+	[[Category: Adenosine triphosphatase]]
		+	[[Category: Dna binding protein]]
		+	[[Category: Dna repair]]
		+	[[Category: Fungal protein]]

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

OCA — Wed, 06 Nov 2013 07:08:52 GMT

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

←Older revision

Revision as of 07:08, 6 November 2013

OCA: New page: '''Unreleased structure''' The entry 4nck is ON HOLD Authors: Classen, S., Williams, G.J., Arvai, A.S., Williams, R.S. Description: Crystal Structure of Pyrococcus furiosis Rad50 R797G...

OCA — Wed, 06 Nov 2013 07:08:52 GMT

New page: '''Unreleased structure''' The entry 4nck is ON HOLD Authors: Classen, S., Williams, G.J., Arvai, A.S., Williams, R.S. Description: Crystal Structure of Pyrococcus furiosis Rad50 R797G...

New page

'''Unreleased structure'''

The entry 4nck is ON HOLD

Authors: Classen, S., Williams, G.J., Arvai, A.S., Williams, R.S.

Description: Crystal Structure of Pyrococcus furiosis Rad50 R797G mutation