3t3k - Revision history

OCA at 10:02, 1 March 2024

2024-03-01T10:02:06Z

←Older revision		Revision as of 10:02, 1 March 2024
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	<StructureSection load='3t3k' size='340' side='right'caption='[[3t3k]], [[Resolution\|resolution]] 1.24Å' scene=''>		<StructureSection load='3t3k' size='340' side='right'caption='[[3t3k]], [[Resolution\|resolution]] 1.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t3k]] is a 1 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=3T3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3K FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[3t3j\|3t3j]], [[3t3l\|3t3l]], [[3t3t\|3t3t]], [[3t3x\|3t3x]]</div></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]] 1.24Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">FXN, FRDA, X25 ([https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [https://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=3t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3k OCA], [https://pdbe.org/3t3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3k RCSB], [https://www.ebi.ac.uk/pdbsum/3t3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3k 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=3t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3k OCA], [https://pdbe.org/3t3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3k RCSB], [https://www.ebi.ac.uk/pdbsum/3t3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3k ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[https://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref> <ref>PMID:9779809</ref> <ref>PMID:10732799</ref> <ref>PMID:9989622</ref> [:]<ref>PMID:10874325</ref> <ref>PMID:19629184</ref>	+	[https://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[https://omim.org/entry/229300 229300]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref> <ref>PMID:9779809</ref> <ref>PMID:10732799</ref> <ref>PMID:9989622</ref> [:]<ref>PMID:10874325</ref> <ref>PMID:19629184</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref> <ref>PMID:11823441</ref> <ref>PMID:12755598</ref> <ref>PMID:12785837</ref> <ref>PMID:15123683</ref> <ref>PMID:15247478</ref> <ref>PMID:15641778</ref> <ref>PMID:16239244</ref> <ref>PMID:16608849</ref>	+	[https://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref> <ref>PMID:11823441</ref> <ref>PMID:12755598</ref> <ref>PMID:12785837</ref> <ref>PMID:15123683</ref> <ref>PMID:15247478</ref> <ref>PMID:15641778</ref> <ref>PMID:16239244</ref> <ref>PMID:16608849</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Friedreich's ataxia (FRDA) is a progressive neurodegenerative disease associated with the loss of function of the protein frataxin (FXN) that results from low FXN levels due to a GAA triplet repeat expansion or, occasionally, from missense mutations in the FXN gene. Here biochemical and structural properties of FXN variants, including three FRDA missense mutations (N146K, Q148R, and R165C) and three related mutants (N146A, Q148G, and Q153A), were determined in an effort to understand the structural basis for the loss of function. In vitro assays revealed that although the three FRDA missense mutations exhibited similar losses of cysteine desulfurase and Fe-S cluster assembly activities, the causes for these activation defects were distinct. The R165C variant exhibited a k(cat)/K(M) higher than that of native FXN but weak binding to the NFS1, ISD11, and ISCU2 (SDU) complex, whereas the Q148R variant exhibited the lowest k(cat)/K(M) of the six tested FXN variants and only a modest binding deficiency. The order of the FXN binding affinities for the SDU Fe-S assembly complex was as follows: FXN > Q148R > N146A > Q148G > N146K > Q153A > R165C. Four different classes of FXN variants were identified on the basis of their biochemical properties. Together, these structure-function studies reveal determinants for the binding and allosteric activation of the Fe-S assembly complex and provide insight into how FRDA missense mutations are functionally compromised.	+
-		+
-	Structure-Function Analysis of Friedreich's Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe-S Assembly Complex.,Bridwell-Rabb J, Winn AM, Barondeau DP Biochemistry. 2011 Aug 2. PMID:21776984<ref>PMID:21776984</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3t3k" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ferroxidase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Barondeau~~, D P~~]]	+	[[Category: Barondeau DP]]
-	[[Category: Bridwell-Rabb, J]]	+	[[Category: Bridwell-Rabb J]]
-	[[Category: Winn~~, A M]]~~	+	[[Category: Winn AM]]
-	~~[[Category: Fe-s cluster biosynthesis]]~~	+
-	~~[[Category: Human mitochondria]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 16:41, 6 July 2022

2022-07-06T16:41:29Z

←Older revision		Revision as of 16:41, 6 July 2022
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	==1.24 A Structure of Friedreich's ataxia frataxin variant Q148R==		==1.24 A Structure of Friedreich's ataxia frataxin variant Q148R==
-	<StructureSection load='3t3k' size='340' side='right' caption='[[3t3k]], [[Resolution\|resolution]] 1.24Å' scene=''>	+	<StructureSection load='3t3k' size='340' side='right'caption='[[3t3k]], [[Resolution\|resolution]] 1.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t3k]] is a 1 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=3T3K OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3T3K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3K FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3t3j\|3t3j]], [[3t3l\|3t3l]], [[3t3t\|3t3t]], [[3t3x\|3t3x]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3t3j\|3t3j]], [[3t3l\|3t3l]], [[3t3t\|3t3t]], [[3t3x\|3t3x]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FXN, FRDA, X25 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FXN, FRDA, X25 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[https://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [https://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=3t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3k OCA], [~~http~~://pdbe.org/3t3k PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3t3k RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3t3k PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3k 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=3t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3k OCA], [https://pdbe.org/3t3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3k RCSB], [https://www.ebi.ac.uk/pdbsum/3t3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3k ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[~~http~~://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref> <ref>PMID:9779809</ref> <ref>PMID:10732799</ref> <ref>PMID:9989622</ref> [:]<ref>PMID:10874325</ref> <ref>PMID:19629184</ref>	+	[[https://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[https://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref> <ref>PMID:9779809</ref> <ref>PMID:10732799</ref> <ref>PMID:9989622</ref> [:]<ref>PMID:10874325</ref> <ref>PMID:19629184</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref> <ref>PMID:11823441</ref> <ref>PMID:12755598</ref> <ref>PMID:12785837</ref> <ref>PMID:15123683</ref> <ref>PMID:15247478</ref> <ref>PMID:15641778</ref> <ref>PMID:16239244</ref> <ref>PMID:16608849</ref>	+	[[https://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref> <ref>PMID:11823441</ref> <ref>PMID:12755598</ref> <ref>PMID:12785837</ref> <ref>PMID:15123683</ref> <ref>PMID:15247478</ref> <ref>PMID:15641778</ref> <ref>PMID:16239244</ref> <ref>PMID:16608849</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 3t3k" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3t3k" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Frataxin 3D Structures\|Frataxin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 31:
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Barondeau, D P]]		[[Category: Barondeau, D P]]
	[[Category: Bridwell-Rabb, J]]		[[Category: Bridwell-Rabb, J]]

OCA at 12:52, 4 August 2016

2016-08-04T12:52:01Z

←Older revision		Revision as of 12:52, 4 August 2016
Line 1:		Line 1:
		+
	==1.24 A Structure of Friedreich's ataxia frataxin variant Q148R==		==1.24 A Structure of Friedreich's ataxia frataxin variant Q148R==
	<StructureSection load='3t3k' size='340' side='right' caption='[[3t3k]], [[Resolution\|resolution]] 1.24Å' scene=''>		<StructureSection load='3t3k' size='340' side='right' caption='[[3t3k]], [[Resolution\|resolution]] 1.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t3k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T3K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t3k]] is a 1 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=3T3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T3K FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3t3j\|3t3j]], [[3t3l\|3t3l]], [[3t3t\|3t3t]], [[3t3x\|3t3x]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3t3j\|3t3j]], [[3t3l\|3t3l]], [[3t3t\|3t3t]], [[3t3x\|3t3x]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FXN, FRDA, X25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FXN, FRDA, X25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t3k RCSB], [http://www.ebi.ac.uk/pdbsum/3t3k 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=3t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3k OCA], [http://pdbe.org/3t3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t3k RCSB], [http://www.ebi.ac.uk/pdbsum/3t3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3k ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 3t3k" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Barondeau, D P]]		[[Category: Barondeau, D P]]
	[[Category: Bridwell-Rabb, J]]		[[Category: Bridwell-Rabb, J]]

OCA at 07:16, 21 December 2014

2014-12-21T07:16:56Z

←Older revision		Revision as of 07:16, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3t3k\| PDB=3t3k \| SCENE= }}~~	+	==1.24 A Structure of Friedreich's ataxia frataxin variant Q148R==
-	===1.24 A Structure of Friedreich's ataxia frataxin variant Q148R===	+	<StructureSection load='3t3k' size='340' side='right' caption='[[3t3k]], [[Resolution\|resolution]] 1.24Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21776984}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3t3k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T3K FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3t3j\|3t3j]], [[3t3l\|3t3l]], [[3t3t\|3t3t]], [[3t3x\|3t3x]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FXN, FRDA, X25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t3k RCSB], [http://www.ebi.ac.uk/pdbsum/3t3k PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[http://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref> <ref>PMID:9779809</ref> <ref>PMID:10732799</ref> <ref>PMID:9989622</ref> [:]<ref>PMID:10874325</ref> <ref>PMID:19629184</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref> <ref>PMID:11823441</ref> <ref>PMID:12755598</ref> <ref>PMID:12785837</ref> <ref>PMID:15123683</ref> <ref>PMID:15247478</ref> <ref>PMID:15641778</ref> <ref>PMID:16239244</ref> <ref>PMID:16608849</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Friedreich's ataxia (FRDA) is a progressive neurodegenerative disease associated with the loss of function of the protein frataxin (FXN) that results from low FXN levels due to a GAA triplet repeat expansion or, occasionally, from missense mutations in the FXN gene. Here biochemical and structural properties of FXN variants, including three FRDA missense mutations (N146K, Q148R, and R165C) and three related mutants (N146A, Q148G, and Q153A), were determined in an effort to understand the structural basis for the loss of function. In vitro assays revealed that although the three FRDA missense mutations exhibited similar losses of cysteine desulfurase and Fe-S cluster assembly activities, the causes for these activation defects were distinct. The R165C variant exhibited a k(cat)/K(M) higher than that of native FXN but weak binding to the NFS1, ISD11, and ISCU2 (SDU) complex, whereas the Q148R variant exhibited the lowest k(cat)/K(M) of the six tested FXN variants and only a modest binding deficiency. The order of the FXN binding affinities for the SDU Fe-S assembly complex was as follows: FXN > Q148R > N146A > Q148G > N146K > Q153A > R165C. Four different classes of FXN variants were identified on the basis of their biochemical properties. Together, these structure-function studies reveal determinants for the binding and allosteric activation of the Fe-S assembly complex and provide insight into how FRDA missense mutations are functionally compromised.

-	~~==Disease==~~	+	Structure-Function Analysis of Friedreich's Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe-S Assembly Complex.,Bridwell-Rabb J, Winn AM, Barondeau DP Biochemistry. 2011 Aug 2. PMID:21776984<ref>PMID:21776984</ref>
-	~~[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause~~ of Friedreich ~~ataxia (FRDA) [MIM:[http://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration~~ and ~~cardiomyopathy it is~~ the ~~most common inherited ataxia~~. ~~The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements~~, ~~dysarthria~~, ~~nystagmus~~, ~~diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe~~. ~~In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene~~. ~~But in some cases the disease is due to mutations in the coding region.[:][:]<ref>~~PMID:~~9150176</ref><ref>PMID:9779809</ref><ref>PMID:10732799</ref><ref>PMID:9989622</ref>[:]<ref>PMID:10874325</ref>~~<ref>PMID:~~19629184~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play~~ a ~~role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation~~ of ~~Fe(2+) to Fe(3+); the oligomeric form but not~~ the ~~monomeric form has in vitro ferroxidase activity~~. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. ~~Modulates the RNA-binding activity~~ of ~~ACO1~~.<~~ref~~>~~PMID:20053667~~</~~ref~~>~~<ref>PMID:11823441</ref><ref>PMID:12755598</ref><ref>PMID:12785837</ref><ref>PMID:15123683</ref><ref>PMID:15247478</ref><ref>PMID:15641778</ref><ref>PMID:16239244</ref><ref>PMID:16608849</ref>~~	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	[[3t3k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3K OCA].	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+
-	~~<ref group="xtra">PMID:021776984</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Barondeau, D P.]]	+	[[Category: Barondeau, D P]]
-	[[Category: Bridwell-Rabb, J.]]	+	[[Category: Bridwell-Rabb, J]]
-	[[Category: Winn, A M.]]	+	[[Category: Winn, A M]]
	[[Category: Fe-s cluster biosynthesis]]		[[Category: Fe-s cluster biosynthesis]]
	[[Category: Human mitochondria]]		[[Category: Human mitochondria]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 18:52, 24 March 2013

2013-03-24T18:52:59Z

←Older revision		Revision as of 18:52, 24 March 2013
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-	[[Image:3t3k.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3t3k", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3t3k\| PDB=3t3k \| SCENE= }}		{{STRUCTURE_3t3k\| PDB=3t3k \| SCENE= }}
-
	===1.24 A Structure of Friedreich's ataxia frataxin variant Q148R===		===1.24 A Structure of Friedreich's ataxia frataxin variant Q148R===
		+	{{ABSTRACT_PUBMED_21776984}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[http://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref><ref>PMID:9779809</ref><ref>PMID:10732799</ref><ref>PMID:9989622</ref>[:]<ref>PMID:10874325</ref><ref>PMID:19629184</ref>

-	~~<!--~~	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21776984}}, adds the Publication Abstract to the page~~	+	[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref><ref>PMID:11823441</ref><ref>PMID:12755598</ref><ref>PMID:12785837</ref><ref>PMID:15123683</ref><ref>PMID:15247478</ref><ref>PMID:15641778</ref><ref>PMID:16239244</ref><ref>PMID:16608849</ref>
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~), ~~where 21776984~~ is the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_21776984}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021776984</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021776984</ref><references group="xtra"/><references/>
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 06:01, 31 August 2011

2011-08-31T06:01:19Z

←Older revision		Revision as of 06:01, 31 August 2011
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-	[[Image:3t3k.~~jpg~~\|left\|200px]]	+	[[Image:3t3k.png\|left\|200px]]

	<!--		<!--

OCA at 06:03, 10 August 2011

2011-08-10T06:03:02Z

←Older revision		Revision as of 06:03, 10 August 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:3t3k.jpg\|left\|200px]]

-	The ~~entry 3t3k~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3t3k", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3t3k\| PDB=3t3k \| SCENE= }}

-	~~Authors: Bridwell-Rabb, J~~.	+	===1.24 A Structure of Friedreich's ataxia frataxin variant Q148R===

-	~~Description~~: 1.24 A ~~Structure of Friedreich'~~s ~~ataxia frataxin variant Q148R~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21776984}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21776984 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21776984}}
		+
		+	==About this Structure==
		+	[[3t3k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3K OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021776984</ref><references group="xtra"/>
		+	[[Category: Ferroxidase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Barondeau, D P.]]
		+	[[Category: Bridwell-Rabb, J.]]
		+	[[Category: Winn, A M.]]
		+	[[Category: Fe-s cluster biosynthesis]]
		+	[[Category: Human mitochondria]]
		+	[[Category: Oxidoreductase]]

OCA: Protected "3t3k" [edit=sysop:move=sysop]

2011-08-03T08:25:36Z

Protected "3t3k" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:25, 3 August 2011

OCA: New page: '''Unreleased structure''' The entry 3t3k is ON HOLD Authors: Bridwell-Rabb, J. Description: 1.24 A Structure of Friedreich's ataxia frataxin variant Q148R

2011-08-03T08:25:34Z

New page: '''Unreleased structure''' The entry 3t3k is ON HOLD Authors: Bridwell-Rabb, J. Description: 1.24 A Structure of Friedreich's ataxia frataxin variant Q148R

New page

'''Unreleased structure'''

The entry 3t3k is ON HOLD

Authors: Bridwell-Rabb, J.

Description: 1.24 A Structure of Friedreich's ataxia frataxin variant Q148R