3t3t - Revision history

OCA at 10:02, 1 March 2024

OCA — Fri, 01 Mar 2024 10:02:14 GMT

←Older revision		Revision as of 10:02, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3t3t' size='340' side='right'caption='[[3t3t]], [[Resolution\|resolution]] 1.38Å' scene=''>		<StructureSection load='3t3t' size='340' side='right'caption='[[3t3t]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t3t]] is a 4 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=3T3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t3t]] is a 4 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=3T3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3T FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<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]] 1.38Å</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]]~~, [[~~3t3k~~\|~~3t3k~~]]~~, [[3t3l\|3t3l]], [[3t3x\|3t3x]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3t OCA], [https://pdbe.org/3t3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3t RCSB], [https://www.ebi.ac.uk/pdbsum/3t3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3t 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=3t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3t OCA], [https://pdbe.org/3t3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3t RCSB], [https://www.ebi.ac.uk/pdbsum/3t3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3t 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 3t3t" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 30:		Line 19:
	__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

OCA — Wed, 06 Jul 2022 16:41:54 GMT

←Older revision		Revision as of 16:41, 6 July 2022
Line 1:		Line 1:

	==1.38 A structure of human frataxin variant Q148G==		==1.38 A structure of human frataxin variant Q148G==
-	<StructureSection load='3t3t' size='340' side='right' caption='[[3t3t]], [[Resolution\|resolution]] 1.38Å' scene=''>	+	<StructureSection load='3t3t' size='340' side='right'caption='[[3t3t]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t3t]] is a 4 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=3T3T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3T3T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t3t]] is a 4 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=3T3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3t3j\|3t3j]], [[3t3k\|3t3k]], [[3t3l\|3t3l]], [[3t3x\|3t3x]]</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]], [[3t3k\|3t3k]], [[3t3l\|3t3l]], [[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=3t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3t OCA], [~~http~~://pdbe.org/3t3t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3t3t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3t3t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3t 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=3t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3t OCA], [https://pdbe.org/3t3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3t RCSB], [https://www.ebi.ac.uk/pdbsum/3t3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3t 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 ==
Line 23:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 3t3t" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3t3t" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Frataxin 3D Structures\|Frataxin 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 32:
	[[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 17:13, 5 August 2016

OCA — Fri, 05 Aug 2016 17:13:38 GMT

←Older revision		Revision as of 17:13, 5 August 2016
Line 1:		Line 1:
		+
	==1.38 A structure of human frataxin variant Q148G==		==1.38 A structure of human frataxin variant Q148G==
	<StructureSection load='3t3t' size='340' side='right' caption='[[3t3t]], [[Resolution\|resolution]] 1.38Å' scene=''>		<StructureSection load='3t3t' size='340' side='right' caption='[[3t3t]], [[Resolution\|resolution]] 1.38Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3t3t]] is a 4 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=3T3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T3T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3t3t]] is a 4 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=3T3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T3T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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"><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">[[3t3j\|3t3j]], [[3t3k\|3t3k]], [[3t3l\|3t3l]], [[3t3x\|3t3x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3t3j\|3t3j]], [[3t3k\|3t3k]], [[3t3l\|3t3l]], [[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=3t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t3t RCSB], [http://www.ebi.ac.uk/pdbsum/3t3t 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=3t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3t OCA], [http://pdbe.org/3t3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t3t RCSB], [http://www.ebi.ac.uk/pdbsum/3t3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3t ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	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 3t3t" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 28:
	</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 06:51, 21 December 2014

OCA — Sun, 21 Dec 2014 06:51:21 GMT

←Older revision		Revision as of 06:51, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3t3t~~\| ~~PDB~~=3t3t \| ~~SCENE~~= }}	+	==1.38 A structure of human frataxin variant Q148G==
-	===1.~~38 A structure~~ of ~~human~~ frataxin ~~variant Q148G~~===	+	<StructureSection load='3t3t' size='340' side='right' caption='[[3t3t]], [[Resolution\|resolution]] 1.38Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21776984}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3t3t]] is a 4 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=3T3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T3T FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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">[[3t3j\|3t3j]], [[3t3k\|3t3k]], [[3t3l\|3t3l]], [[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=3t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t3t RCSB], [http://www.ebi.ac.uk/pdbsum/3t3t 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/>
-	[[3t3t]] is a 4 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=3T3T 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 02:17, 25 March 2013

OCA — Mon, 25 Mar 2013 02:17:12 GMT

←Older revision		Revision as of 02:17, 25 March 2013
Line 1:		Line 1:
-	[[Image:3t3t.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3t3t", 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_3t3t\| PDB=3t3t \| SCENE= }}		{{STRUCTURE_3t3t\| PDB=3t3t \| SCENE= }}
-
	===1.38 A structure of human frataxin variant Q148G===		===1.38 A structure of human frataxin variant Q148G===
		+	{{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 05:43, 31 August 2011

OCA — Wed, 31 Aug 2011 05:43:34 GMT

←Older revision		Revision as of 05:43, 31 August 2011
Line 1:		Line 1:
-	[[Image:3t3t.~~jpg~~\|left\|200px]]	+	[[Image:3t3t.png\|left\|200px]]

	<!--		<!--

OCA at 05:55, 10 August 2011

OCA — Wed, 10 Aug 2011 05:55:11 GMT

←Older revision		Revision as of 05:55, 10 August 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3t3t.jpg\|left\|200px]]

-	The ~~entry 3t3t~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3t3t", 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_3t3t\| PDB=3t3t \| SCENE= }}

-	~~Authors: Bridwell-Rabb, J~~.~~, Winn,~~ A~~.M., Barondeau, D.P.~~	+	===1.38 A structure of human frataxin variant Q148G===

-	~~Description~~: 1.~~38 A~~ structure ~~of human frataxin variant Q148G~~	+
		+	<!--
		+	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==
		+	[[3t3t]] is a 4 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=3T3T 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 "3t3t" [edit=sysop:move=sysop]

OCA — Wed, 03 Aug 2011 08:25:52 GMT

Protected "3t3t" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:25, 3 August 2011

OCA: New page: '''Unreleased structure''' The entry 3t3t is ON HOLD Authors: Bridwell-Rabb, J., Winn, A.M., Barondeau, D.P. Description: 1.38 A structure of human frataxin variant Q148G

OCA — Wed, 03 Aug 2011 08:25:51 GMT

New page: '''Unreleased structure''' The entry 3t3t is ON HOLD Authors: Bridwell-Rabb, J., Winn, A.M., Barondeau, D.P. Description: 1.38 A structure of human frataxin variant Q148G

New page

'''Unreleased structure'''

The entry 3t3t is ON HOLD

Authors: Bridwell-Rabb, J., Winn, A.M., Barondeau, D.P.

Description: 1.38 A structure of human frataxin variant Q148G