5tre - Revision history

OCA at 12:12, 6 November 2024

2024-11-06T12:12:49Z

← Older revision		Revision as of 12:12, 6 November 2024
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ISU1_YEAST ISU1_YEAST] Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (PubMed:10588895, PubMed:12970193, PubMed:14741370, PubMed:15123690, PubMed:16341089, PubMed:16431909, PubMed:23615440, PubMed:25358379).<ref>PMID:10588895</ref> <ref>PMID:12970193</ref> <ref>PMID:14741370</ref> <ref>PMID:15123690</ref> <ref>PMID:16341089</ref> <ref>PMID:16431909</ref> <ref>PMID:23615440</ref> <ref>PMID:25358379</ref>		[https://www.uniprot.org/uniprot/ISU1_YEAST ISU1_YEAST] Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (PubMed:10588895, PubMed:12970193, PubMed:14741370, PubMed:15123690, PubMed:16341089, PubMed:16431909, PubMed:23615440, PubMed:25358379).<ref>PMID:10588895</ref> <ref>PMID:12970193</ref> <ref>PMID:14741370</ref> <ref>PMID:15123690</ref> <ref>PMID:16341089</ref> <ref>PMID:16431909</ref> <ref>PMID:23615440</ref> <ref>PMID:25358379</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Early studies of the bacterial Fe-S cluster assembly system provided structural details for how the scaffold protein and the cysteine desulfurase interact. This work and additional work on the yeast and human systems elucidated a conserved mechanism for sulfur donation but did not provide any conclusive insights into the mechanism for iron delivery from the iron donor, frataxin, to the scaffold. We previously showed that oligomerization is a mechanism by which yeast frataxin (Yfh1) can promote assembly of the core machinery for Fe-S cluster synthesis both in vitro and in cells, in such a manner that the scaffold protein, Isu1, can bind to Yfh1 independent of the presence of the cysteine desulfurase, Nfs1. Here, in the absence of Yfh1, Isu1 was found to exist in two forms, one mostly monomeric with limited tendency to dimerize, and one with a strong propensity to oligomerize. Whereas the monomeric form is stabilized by zinc, the loss of zinc promotes formation of dimer and higher order oligomers. However, upon binding to oligomeric Yfh1, both forms take on a similar symmetrical trimeric configuration that places the Fe-S cluster coordinating residues of Isu1 in close proximity of iron-binding residues of Yfh1. This configuration is suitable for docking of Nfs1 in a manner that provides a structural context for coordinate iron and sulfur donation to the scaffold. Moreover, distinct structural features suggest that in physiological conditions the zinc-regulated abundance of monomeric vs. oligomeric Isu1 yields [Yfh1].[Isu1] complexes with different Isu1 configurations that afford unique functional properties for Fe-S cluster assembly and delivery.

			Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe-S cluster assembly centers.,Galeano BK, Ranatunga W, Gakh O, Smith DY, Thompson JR, Isaya G Metallomics. 2017 Jun 21;9(6):773-801. doi: 10.1039/c7mt00089h. PMID:28548666<ref>PMID:28548666</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 5tre" style="background-color:#fffaf0;"></div>

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

OCA at 15:42, 6 March 2024

2024-03-06T15:42:48Z

← Older revision		Revision as of 15:42, 6 March 2024
Line 3:		Line 3:
	<SX load='5tre' size='340' side='right' viewer='molstar' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>		<SX load='5tre' size='340' side='right' viewer='molstar' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5TRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TRE FirstGlance]. <br>
	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ISU1, NUA1, YPL135W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=4932 ATCC 18824]), YFH1, YDL120W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>~~		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 15.6Å</td></tr>
	~~<tr id='activity'><td class~~="~~sblockLbl~~">~~<b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>~~[~~http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase~~]~~, with EC number [http://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5tre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tre OCA], [https://pdbe.org/5tre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tre RCSB], [https://www.ebi.ac.uk/pdbsum/5tre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tre 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=5tre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tre OCA], [~~http~~://pdbe.org/5tre PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tre RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tre PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tre ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/ISU1_YEAST ISU1_YEAST]] Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (PubMed:10588895, PubMed:12970193, PubMed:14741370, PubMed:15123690, PubMed:16341089, PubMed:16431909, PubMed:23615440, PubMed:25358379).<ref>PMID:10588895</ref> <ref>PMID:12970193</ref> <ref>PMID:14741370</ref> <ref>PMID:15123690</ref> <ref>PMID:16341089</ref> <ref>PMID:16431909</ref> <ref>PMID:23615440</ref> <ref>PMID:25358379</ref> [[http://www.uniprot.org/uniprot/FRDA_YEAST FRDA_YEAST]] Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. Plays a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). Can store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. May be involved in regulation of the mitochondrial electron transport chain.<ref>PMID:9180083</ref> <ref>PMID:9988680</ref> <ref>PMID:15961414</ref> <ref>PMID:16371422</ref> <ref>PMID:19884169</ref> <ref>PMID:17027502</ref>		[https://www.uniprot.org/uniprot/ISU1_YEAST ISU1_YEAST] Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (PubMed:10588895, PubMed:12970193, PubMed:14741370, PubMed:15123690, PubMed:16341089, PubMed:16431909, PubMed:23615440, PubMed:25358379).<ref>PMID:10588895</ref> <ref>PMID:12970193</ref> <ref>PMID:14741370</ref> <ref>PMID:15123690</ref> <ref>PMID:16341089</ref> <ref>PMID:16431909</ref> <ref>PMID:23615440</ref> <ref>PMID:25358379</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Early studies of the bacterial Fe-S cluster assembly system provided structural details for how the scaffold protein and the cysteine desulfurase interact. This work and additional work on the yeast and human systems elucidated a conserved mechanism for sulfur donation but did not provide any conclusive insights into the mechanism for iron delivery from the iron donor, frataxin, to the scaffold. We previously showed that oligomerization is a mechanism by which yeast frataxin (Yfh1) can promote assembly of the core machinery for Fe-S cluster synthesis both in vitro and in cells, in such a manner that the scaffold protein, Isu1, can bind to Yfh1 independent of the presence of the cysteine desulfurase, Nfs1. Here, in the absence of Yfh1, Isu1 was found to exist in two forms, one mostly monomeric with limited tendency to dimerize, and one with a strong propensity to oligomerize. Whereas the monomeric form is stabilized by zinc, the loss of zinc promotes formation of dimer and higher order oligomers. However, upon binding to oligomeric Yfh1, both forms take on a similar symmetrical trimeric configuration that places the Fe-S cluster coordinating residues of Isu1 in close proximity of iron-binding residues of Yfh1. This configuration is suitable for docking of Nfs1 in a manner that provides a structural context for coordinate iron and sulfur donation to the scaffold. Moreover, distinct structural features suggest that in physiological conditions the zinc-regulated abundance of monomeric vs. oligomeric Isu1 yields [Yfh1].[Isu1] complexes with different Isu1 configurations that afford unique functional properties for Fe-S cluster assembly and delivery.

	Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe-S cluster assembly centers.,Galeano BK, Ranatunga W, Gakh O, Smith DY, Thompson JR, Isaya G Metallomics. 2017 Jun 21;9(6):773-801. doi: 10.1039/c7mt00089h. PMID:28548666<ref>PMID:28548666</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 5tre" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==
Line 26:		Line 16:
	__TOC__		__TOC__
	</SX>		</SX>
	~~[[Category: Atcc 18824]]~~
	~~[[Category: Ferroxidase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Gakh, O~~]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: ~~Galeano, B K~~]]		[[Category: Gakh O]]
	[[Category: ~~IV, D Y.Smith~~]]		[[Category: Galeano BK]]
	[[Category: Isaya, G]]		[[Category: Isaya G]]
	[[Category: Ranatunga, W]]		[[Category: Ranatunga W]]
	[[Category: ~~Thompson, J R~~]]		[[Category: Smith IV DY]]
	[[Category: ~~Frataxin]]~~		[[Category: Thompson JR]]
	~~[[Category: Friedreich ataxia]]~~
	~~[[Category: Iron-sulfur protein]]~~
	~~[[Category: Mitochondria]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Protein complex~~]]

OCA at 21:46, 10 April 2020

2020-04-10T21:46:50Z

← Older revision		Revision as of 21:46, 10 April 2020
Line 3:		Line 3:
	<SX load='5tre' size='340' side='right' viewer='molstar' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>		<SX load='5tre' size='340' side='right' viewer='molstar' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TRE FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ISU1, NUA1, YPL135W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), YFH1, YDL120W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ISU1, NUA1, YPL135W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), YFH1, YDL120W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5tre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tre OCA], [http://pdbe.org/5tre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tre RCSB], [http://www.ebi.ac.uk/pdbsum/5tre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tre 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=5tre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tre OCA], [http://pdbe.org/5tre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tre RCSB], [http://www.ebi.ac.uk/pdbsum/5tre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tre ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 19:38, 6 March 2020

2020-03-06T19:38:30Z

← Older revision		Revision as of 19:38, 6 March 2020
Line 1:		Line 1:

	==Zinc and the Iron Donor Frataxin Regulate Oligomerization of the Scaffold Protein to Form New Fe-S Cluster Assembly Centers==		==Zinc and the Iron Donor Frataxin Regulate Oligomerization of the Scaffold Protein to Form New Fe-S Cluster Assembly Centers==
	<~~StructureSection~~ load='5tre' size='340' side='right'caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>		<SX load='5tre' size='340' side='right' viewer='molstar' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRE FirstGlance]. <br>
Line 25:		Line 25:
	<references/>		<references/>
	__TOC__		__TOC__
	</~~StructureSection~~>		</SX>
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]

OCA at 09:03, 18 December 2019

2019-12-18T09:03:02Z

← Older revision		Revision as of 09:03, 18 December 2019
Line 1:		Line 1:

	==Zinc and the Iron Donor Frataxin Regulate Oligomerization of the Scaffold Protein to Form New Fe-S Cluster Assembly Centers==		==Zinc and the Iron Donor Frataxin Regulate Oligomerization of the Scaffold Protein to Form New Fe-S Cluster Assembly Centers==
	<StructureSection load='5tre' size='340' side='right' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>		<StructureSection load='5tre' size='340' side='right'caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRE FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5tre" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tre" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Frataxin 3D Structures\|Frataxin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 28:
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
			[[Category: Large Structures]]
	[[Category: Gakh, O]]		[[Category: Gakh, O]]
	[[Category: Galeano, B K]]		[[Category: Galeano, B K]]

OCA at 09:08, 18 July 2018

2018-07-18T09:08:06Z

← Older revision		Revision as of 09:08, 18 July 2018
Line 3:		Line 3:
	<StructureSection load='5tre' size='340' side='right' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>		<StructureSection load='5tre' size='340' side='right' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRE FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ISU1, NUA1, YPL135W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), YFH1, YDL120W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5tre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tre OCA], [http://pdbe.org/5tre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tre RCSB], [http://www.ebi.ac.uk/pdbsum/5tre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tre 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=5tre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tre OCA], [http://pdbe.org/5tre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tre RCSB], [http://www.ebi.ac.uk/pdbsum/5tre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tre ProSAT]</span></td></tr>
	</table>		</table>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Atcc 18824]]
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Gakh, O]]		[[Category: Gakh, O]]

OCA at 10:40, 13 September 2017

2017-09-13T10:40:47Z

← Older revision		Revision as of 10:40, 13 September 2017
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	~~'''Unreleased structure'''~~

	~~The entry~~ 5tre is ~~ON HOLD~~ ~~until Oct 26 2018~~		==Zinc and the Iron Donor Frataxin Regulate Oligomerization of the Scaffold Protein to Form New Fe-S Cluster Assembly Centers==
			<StructureSection load='5tre' size='340' side='right' caption='[[5tre]], [[Resolution\|resolution]] 15.60Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[5tre]] is a 48 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TRE FirstGlance]. <br>
			</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5tre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tre OCA], [http://pdbe.org/5tre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tre RCSB], [http://www.ebi.ac.uk/pdbsum/5tre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tre ProSAT]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/ISU1_YEAST ISU1_YEAST]] Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (PubMed:10588895, PubMed:12970193, PubMed:14741370, PubMed:15123690, PubMed:16341089, PubMed:16431909, PubMed:23615440, PubMed:25358379).<ref>PMID:10588895</ref> <ref>PMID:12970193</ref> <ref>PMID:14741370</ref> <ref>PMID:15123690</ref> <ref>PMID:16341089</ref> <ref>PMID:16431909</ref> <ref>PMID:23615440</ref> <ref>PMID:25358379</ref> [[http://www.uniprot.org/uniprot/FRDA_YEAST FRDA_YEAST]] Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. Plays a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). Can store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. May be involved in regulation of the mitochondrial electron transport chain.<ref>PMID:9180083</ref> <ref>PMID:9988680</ref> <ref>PMID:15961414</ref> <ref>PMID:16371422</ref> <ref>PMID:19884169</ref> <ref>PMID:17027502</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Early studies of the bacterial Fe-S cluster assembly system provided structural details for how the scaffold protein and the cysteine desulfurase interact. This work and additional work on the yeast and human systems elucidated a conserved mechanism for sulfur donation but did not provide any conclusive insights into the mechanism for iron delivery from the iron donor, frataxin, to the scaffold. We previously showed that oligomerization is a mechanism by which yeast frataxin (Yfh1) can promote assembly of the core machinery for Fe-S cluster synthesis both in vitro and in cells, in such a manner that the scaffold protein, Isu1, can bind to Yfh1 independent of the presence of the cysteine desulfurase, Nfs1. Here, in the absence of Yfh1, Isu1 was found to exist in two forms, one mostly monomeric with limited tendency to dimerize, and one with a strong propensity to oligomerize. Whereas the monomeric form is stabilized by zinc, the loss of zinc promotes formation of dimer and higher order oligomers. However, upon binding to oligomeric Yfh1, both forms take on a similar symmetrical trimeric configuration that places the Fe-S cluster coordinating residues of Isu1 in close proximity of iron-binding residues of Yfh1. This configuration is suitable for docking of Nfs1 in a manner that provides a structural context for coordinate iron and sulfur donation to the scaffold. Moreover, distinct structural features suggest that in physiological conditions the zinc-regulated abundance of monomeric vs. oligomeric Isu1 yields [Yfh1].[Isu1] complexes with different Isu1 configurations that afford unique functional properties for Fe-S cluster assembly and delivery.

	~~Authors:~~ Ranatunga, W., Gakh, O~~., Galeano, B.K.~~, Smith ~~IV, D.Y.~~, Thompson, J.R.~~, Isaya, G~~.		Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe-S cluster assembly centers.,Galeano BK, Ranatunga W, Gakh O, Smith DY, Thompson JR, Isaya G Metallomics. 2017 Jun 21;9(6):773-801. doi: 10.1039/c7mt00089h. PMID:28548666<ref>PMID:28548666</ref>

	~~Description: Zinc and~~ the ~~Iron Donor Frataxin Regulate Oligomerization~~ of ~~the Scaffold Protein to Form New Fe~~-~~S Cluster Assembly Centers~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased Structures~~]]		</div>
			<div class="pdbe-citations 5tre" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Ferroxidase]]
	[[Category: Gakh, O]]		[[Category: Gakh, O]]
	[[Category: ~~Smith Iv~~, ~~D.Y~~]]		[[Category: Galeano, B K]]
	[[Category: ~~Galeano~~, B.K]]		[[Category: IV, D Y.Smith]]
	[[Category: Isaya, G]]		[[Category: Isaya, G]]
	[[Category: Ranatunga, W]]		[[Category: Ranatunga, W]]
	[[Category: Thompson, J.R]]		[[Category: Thompson, J R]]
			[[Category: Frataxin]]
			[[Category: Friedreich ataxia]]
			[[Category: Iron-sulfur protein]]
			[[Category: Mitochondria]]
			[[Category: Oxidoreductase]]
			[[Category: Protein complex]]

OCA at 13:45, 9 March 2017

2017-03-09T13:45:21Z

← Older revision		Revision as of 13:45, 9 March 2017
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	Description: Zinc and the Iron Donor Frataxin Regulate Oligomerization of the Scaffold Protein to Form New Fe-S Cluster Assembly Centers		Description: Zinc and the Iron Donor Frataxin Regulate Oligomerization of the Scaffold Protein to Form New Fe-S Cluster Assembly Centers
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	~~[[Category: Isaya, G]]~~
	~~[[Category: Thompson, J.R]]~~
	[[Category: Gakh, O]]		[[Category: Gakh, O]]
	[[Category: Smith Iv, D.Y]]		[[Category: Smith Iv, D.Y]]
	[[Category: Galeano, B.K]]		[[Category: Galeano, B.K]]
			[[Category: Isaya, G]]
	[[Category: Ranatunga, W]]		[[Category: Ranatunga, W]]
			[[Category: Thompson, J.R]]

OCA at 17:46, 9 December 2016

2016-12-09T17:46:29Z

← Older revision		Revision as of 17:46, 9 December 2016
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 5tre is ON HOLD		The entry 5tre is ON HOLD until Oct 26 2018

	Authors: Ranatunga, W., Gakh, O., Galeano, B.K., Smith IV, D.Y., Thompson, J.R., Isaya, G.		Authors: Ranatunga, W., Gakh, O., Galeano, B.K., Smith IV, D.Y., Thompson, J.R., Isaya, G.

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

2016-11-02T17:04:59Z

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

← Older revision	Revision as of 17:04, 2 November 2016
(No difference)