3u2l - Revision history

OCA at 13:46, 14 March 2024

2024-03-14T13:46:25Z

←Older revision		Revision as of 13:46, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3u2l' size='340' side='right'caption='[[3u2l]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3u2l' size='340' side='right'caption='[[3u2l]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2L FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FAD:FLAVIN~~-~~ADENINE+DINUCLEOTIDE'>FAD</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]] 1.95Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3o55\|3o55]], [[3u2m\|3u2m]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>GFER, ALR, HERV1, HPO ([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/Thiol_oxidase Thiol oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2]~~ </~~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=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [https://pdbe.org/3u2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [https://www.ebi.ac.uk/pdbsum/3u2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2l 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=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [https://pdbe.org/3u2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [https://www.ebi.ac.uk/pdbsum/3u2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2l ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref>	+	[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN] Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR. The flavoprotein ALR receives two electrons per subunit from Mia40, which are then donated through one-electron reactions to two cytochrome c molecules, thus mediating a switch from two-electron to one-electron transfer. We dissect here the mechanism of the electron flux within ALR, characterizing at the atomic level the ALR intermediates that allow electrons to rapidly flow to cytochrome c. The intermediate critical for the electron-transfer process implies the formation of a specific inter-subunit disulfide which exclusively allows electron flow from Mia40 to FAD. This finding allows us to present a complete model for the electron-transfer pathway in ALR.	+
-		+
-	An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR.,Banci L, Bertini I, Calderone V, Cefaro C, Ciofi-Baffoni S, Gallo A, Tokatlidis K J Am Chem Soc. 2012 Jan 25;134(3):1442-5. Epub 2012 Jan 6. PMID:22224850<ref>PMID:22224850</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3u2l" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 30:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Thiol oxidase]]~~	+	[[Category: Banci L]]
-	[[Category: Banci, L]]	+	[[Category: Bertini I]]
-	[[Category: Bertini, I]]	+	[[Category: Calderone V]]
-	[[Category: Calderone, V]]	+	[[Category: Cefaro C]]
-	[[Category: Cefaro, C]]	+	[[Category: Ciofi-Baffoni S]]
-	[[Category: Ciofi-Baffoni, S]]	+	[[Category: Gallo A]]
-	[[Category: Gallo, A]]	+
-	~~[[Category: Alr]]~~	+
-	~~[[Category: Fad]]~~	+
-	~~[[Category: Flavin]]~~	+
-	~~[[Category: Flavoprotein]]~~	+
-	~~[[Category: Sulfhydryl oxidase~~]]	+

OCA at 05:54, 13 July 2022

2022-07-13T05:54:58Z

←Older revision		Revision as of 05:54, 13 July 2022
Line 1:		Line 1:

	==Crystal structure of human ALR mutant C142S.==		==Crystal structure of human ALR mutant C142S.==
-	<StructureSection load='3u2l' size='340' side='right' caption='[[3u2l]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='3u2l' size='340' side='right'caption='[[3u2l]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3U2L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o55\|3o55]], [[3u2m\|3u2m]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3o55\|3o55]], [[3u2m\|3u2m]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GFER, ALR, HERV1, HPO ([~~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">GFER, ALR, HERV1, HPO ([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/Thiol_oxidase Thiol oxidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [~~http~~://pdbe.org/3u2l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3u2l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2l 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=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [https://pdbe.org/3u2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [https://www.ebi.ac.uk/pdbsum/3u2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2l ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.	+	[[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref>	+	[[https://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</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 3u2l" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3u2l" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Sulfhydryl oxidase 3D structures\|Sulfhydryl oxidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Thiol oxidase]]		[[Category: Thiol oxidase]]
	[[Category: Banci, L]]		[[Category: Banci, L]]

OCA at 09:59, 8 November 2017

2017-11-08T09:59:25Z

←Older revision		Revision as of 09:59, 8 November 2017
Line 23:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 3u2l" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3u2l" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Sulfhydryl oxidase\|Sulfhydryl oxidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:38, 11 August 2016

2016-08-11T16:38:19Z

←Older revision		Revision as of 16:38, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human ALR mutant C142S.==		==Crystal structure of human ALR mutant C142S.==
	<StructureSection load='3u2l' size='340' side='right' caption='[[3u2l]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3u2l' size='340' side='right' caption='[[3u2l]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2L FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o55\|3o55]], [[3u2m\|3u2m]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o55\|3o55]], [[3u2m\|3u2m]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GFER, ALR, HERV1, HPO ([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">GFER, ALR, HERV1, HPO ([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/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [http://www.ebi.ac.uk/pdbsum/3u2l 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=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [http://pdbe.org/3u2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [http://www.ebi.ac.uk/pdbsum/3u2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2l ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 3u2l" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 28:		Line 30:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Thiol oxidase]]		[[Category: Thiol oxidase]]
	[[Category: Banci, L]]		[[Category: Banci, L]]

OCA at 10:03, 4 January 2015

2015-01-04T10:03:46Z

←Older revision		Revision as of 10:03, 4 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2L FirstGlance]. <br>		<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2L FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o55\|3o55]], [[3u2m\|3u2m]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o55\|3o55]], [[3u2m\|3u2m]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GFER, ALR, HERV1, HPO ([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">GFER, ALR, HERV1, HPO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [http://www.ebi.ac.uk/pdbsum/3u2l 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=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [http://www.ebi.ac.uk/pdbsum/3u2l PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.		[[http://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.
Line 19:		Line 19:
	An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR.,Banci L, Bertini I, Calderone V, Cefaro C, Ciofi-Baffoni S, Gallo A, Tokatlidis K J Am Chem Soc. 2012 Jan 25;134(3):1442-5. Epub 2012 Jan 6. PMID:22224850<ref>PMID:22224850</ref>		An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR.,Banci L, Bertini I, Calderone V, Cefaro C, Ciofi-Baffoni S, Gallo A, Tokatlidis K J Am Chem Soc. 2012 Jan 25;134(3):1442-5. Epub 2012 Jan 6. PMID:22224850<ref>PMID:22224850</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>

Line 30:		Line 30:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Thiol oxidase]]		[[Category: Thiol oxidase]]
-	[[Category: Banci, L.]]	+	[[Category: Banci, L]]
-	[[Category: Bertini, I.]]	+	[[Category: Bertini, I]]
-	[[Category: Calderone, V.]]	+	[[Category: Calderone, V]]
-	[[Category: Cefaro, C.]]	+	[[Category: Cefaro, C]]
-	[[Category: Ciofi-Baffoni, S.]]	+	[[Category: Ciofi-Baffoni, S]]
-	[[Category: Gallo, A.]]	+	[[Category: Gallo, A]]
	[[Category: Alr]]		[[Category: Alr]]
	[[Category: Fad]]		[[Category: Fad]]

OCA at 06:39, 5 June 2014

2014-06-05T06:39:25Z

←Older revision		Revision as of 06:39, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3u2l.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of human ALR mutant C142S.==
		+	<StructureSection load='3u2l' size='340' side='right' caption='[[3u2l]], [[Resolution\|resolution]] 1.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3u2l]] 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=3U2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2L FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3o55\|3o55]], [[3u2m\|3u2m]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GFER, ALR, HERV1, HPO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u2l RCSB], [http://www.ebi.ac.uk/pdbsum/3u2l PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ALR_HUMAN ALR_HUMAN]] Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref> Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.<ref>PMID:19397338</ref> <ref>PMID:23186364</ref> <ref>PMID:20593814</ref> <ref>PMID:21383138</ref> <ref>PMID:22224850</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR. The flavoprotein ALR receives two electrons per subunit from Mia40, which are then donated through one-electron reactions to two cytochrome c molecules, thus mediating a switch from two-electron to one-electron transfer. We dissect here the mechanism of the electron flux within ALR, characterizing at the atomic level the ALR intermediates that allow electrons to rapidly flow to cytochrome c. The intermediate critical for the electron-transfer process implies the formation of a specific inter-subunit disulfide which exclusively allows electron flow from Mia40 to FAD. This finding allows us to present a complete model for the electron-transfer pathway in ALR.

-	<!--	+	An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR.,Banci L, Bertini I, Calderone V, Cefaro C, Ciofi-Baffoni S, Gallo A, Tokatlidis K J Am Chem Soc. 2012 Jan 25;134(3):1442-5. Epub 2012 Jan 6. PMID:22224850<ref>PMID:22224850</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3u2l"~~, ~~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_3u2l\| PDB=3u2l \| SCENE= }}~~	+

-	~~===Crystal structure~~ of ~~human ALR mutant C142S~~.~~===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	~~<!--~~	+	*[[Sulfhydryl oxidase\|Sulfhydryl oxidase]]
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22224850}}, adds the Publication Abstract to the page~~	+	== References ==
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 22224850 is the PubMed ID number.~~	+	<references/>
-	~~-->~~	+	__TOC__
-	~~{{ABSTRACT_PUBMED_22224850}}~~	+	</StructureSection>
-		+
-	==~~About this Structure~~==	+
-	[[~~3u2l~~]] 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=3U2L OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022224850<~~/~~ref~~><~~ref group="xtra">PMID:021383138</ref><references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Thiol oxidase]]		[[Category: Thiol oxidase]]

OCA at 07:40, 6 June 2012

2012-06-06T07:40:49Z

←Older revision		Revision as of 07:40, 6 June 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3u2l.jpg\|left\|200px]]

-	The ~~entry 3u2l~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3u2l", 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_3u2l\| PDB=3u2l \| SCENE= }}

-	~~Authors: Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A~~.	+	===Crystal structure of human ALR mutant C142S.===

-	~~Description~~: ~~Crystal~~ structure ~~of human ALR mutant C142S~~.	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22224850}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22224850 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22224850}}
		+
		+	==About this Structure==
		+	[[3u2l]] 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=3U2L OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022224850</ref><ref group="xtra">PMID:021383138</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Thiol oxidase]]
		+	[[Category: Banci, L.]]
		+	[[Category: Bertini, I.]]
		+	[[Category: Calderone, V.]]
		+	[[Category: Cefaro, C.]]
		+	[[Category: Ciofi-Baffoni, S.]]
		+	[[Category: Gallo, A.]]
		+	[[Category: Alr]]
		+	[[Category: Fad]]
		+	[[Category: Flavin]]
		+	[[Category: Flavoprotein]]
		+	[[Category: Sulfhydryl oxidase]]

OCA: Protected "3u2l" [edit=sysop:move=sysop]

2011-10-30T08:48:46Z

Protected "3u2l" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:48, 30 October 2011

OCA: New page: '''Unreleased structure''' The entry 3u2l is ON HOLD until Paper Publication Authors: Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A. Description: Cryst...

2011-10-30T08:48:44Z

New page: '''Unreleased structure''' The entry 3u2l is ON HOLD until Paper Publication Authors: Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A. Description: Cryst...

New page

'''Unreleased structure'''

The entry 3u2l is ON HOLD until Paper Publication

Authors: Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A.

Description: Crystal structure of human ALR mutant C142S.