4wq9 - Revision history

OCA at 11:54, 14 June 2023

OCA — Wed, 14 Jun 2023 11:54:29 GMT

←Older revision		Revision as of 11:54, 14 June 2023
Line 3:		Line 3:
	<StructureSection load='4wq9' size='340' side='right'caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>		<StructureSection load='4wq9' size='340' side='right'caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wq9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Allvd Allvd~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WQ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wq9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Allochromatium_vinosum_DSM_180 Allochromatium vinosum DSM 180]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WQ9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>~~	+
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4wq7\|4wq7]]</div></td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tsdA, Alvin_0091 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=572477 ALLVD])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [https://pdbe.org/4wq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [https://www.ebi.ac.uk/pdbsum/4wq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wq9 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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [https://pdbe.org/4wq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [https://www.ebi.ac.uk/pdbsum/4wq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wq9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TSDA_ALLVD TSDA_ALLVD]] Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.<ref>PMID:16995898</ref> <ref>PMID:22779704</ref>	+	[https://www.uniprot.org/uniprot/TSDA_ALLVD TSDA_ALLVD] Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.<ref>PMID:16995898</ref> <ref>PMID:22779704</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Allvd~~]]	+	[[Category: Allochromatium vinosum DSM 180]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Thiosulfate dehydrogenase]]~~	+	[[Category: Archer M]]
-	[[Category: Archer, M]]	+	[[Category: Brito JA]]
-	[[Category: Brito~~, J A~~]]	+	[[Category: Dahl C]]
-	[[Category: Dahl, C]]	+	[[Category: Denkmann K]]
-	[[Category: Denkmann, K]]	+	[[Category: Pereira IAC]]
-	[[Category: Pereira~~, I A.C]]~~	+
-	~~[[Category: C-type cytochrome]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Tetrathionate]]~~	+
-	~~[[Category: Tsda~~]]	+

OCA at 09:01, 8 September 2021

OCA — Wed, 08 Sep 2021 09:01:22 GMT

←Older revision		Revision as of 09:01, 8 September 2021
Line 1:		Line 1:

	==Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum - dithionite soak==		==Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum - dithionite soak==
-	<StructureSection load='4wq9' size='340' side='right' caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>	+	<StructureSection load='4wq9' size='340' side='right'caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wq9]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Allvd Allvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQ9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4WQ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wq9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Allvd Allvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WQ9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wq7\|4wq7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4wq7\|4wq7]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tsdA, Alvin_0091 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=572477 ALLVD])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tsdA, Alvin_0091 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=572477 ALLVD])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [~~http~~://pdbe.org/4wq9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4wq9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4wq9 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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [https://pdbe.org/4wq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [https://www.ebi.ac.uk/pdbsum/4wq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wq9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TSDA_ALLVD TSDA_ALLVD]] Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.<ref>PMID:16995898</ref> <ref>PMID:22779704</ref>	+	[[https://www.uniprot.org/uniprot/TSDA_ALLVD TSDA_ALLVD]] Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.<ref>PMID:16995898</ref> <ref>PMID:22779704</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Allvd]]		[[Category: Allvd]]
		+	[[Category: Large Structures]]
	[[Category: Thiosulfate dehydrogenase]]		[[Category: Thiosulfate dehydrogenase]]
	[[Category: Archer, M]]		[[Category: Archer, M]]

OCA at 05:57, 8 March 2018

OCA — Thu, 08 Mar 2018 05:57:43 GMT

←Older revision		Revision as of 05:57, 8 March 2018
Line 3:		Line 3:
	<StructureSection load='4wq9' size='340' side='right' caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>		<StructureSection load='4wq9' size='340' side='right' caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wq9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WQ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wq9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Allvd Allvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WQ9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wq7\|4wq7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wq7\|4wq7]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tsdA, Alvin_0091 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=572477 ALLVD])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [http://pdbe.org/4wq9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [http://www.ebi.ac.uk/pdbsum/4wq9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wq9 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [http://pdbe.org/4wq9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [http://www.ebi.ac.uk/pdbsum/4wq9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wq9 ProSAT]</span></td></tr>
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Allvd]]
	[[Category: Thiosulfate dehydrogenase]]		[[Category: Thiosulfate dehydrogenase]]
	[[Category: Archer, M]]		[[Category: Archer, M]]

OCA at 00:20, 26 January 2017

OCA — Thu, 26 Jan 2017 00:20:22 GMT

←Older revision		Revision as of 00:20, 26 January 2017
Line 1:		Line 1:
		+
	==Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum - dithionite soak==		==Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum - dithionite soak==
	<StructureSection load='4wq9' size='340' side='right' caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>		<StructureSection load='4wq9' size='340' side='right' caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wq7\|4wq7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wq7\|4wq7]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [http://www.ebi.ac.uk/pdbsum/4wq9 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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [http://pdbe.org/4wq9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [http://www.ebi.ac.uk/pdbsum/4wq9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wq9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4wq9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:10, 25 February 2015

OCA — Wed, 25 Feb 2015 08:10:16 GMT

←Older revision		Revision as of 08:10, 25 February 2015
Line 13:		Line 13:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~The ability to perform~~ the ~~very simple oxidation~~ of two ~~molecules of~~ thiosulfate to tetrathionate ~~is widespread among prokaryotes. Despite the prevalent occurrence of tetrathionate formation and its~~ well documented ~~significance within~~ the sulfur cycle, little is known about the enzymes ~~that catalyze the oxidative condensation of two thiosulfate anions. To fill~~ this ~~gap~~, the thiosulfate dehydrogenase (TsdA) ~~enzyme from~~ the ~~purple sulfur bacterium Allochromatium~~ vinosum ~~was recombinantly expressed in Escherichia coli~~, ~~purified~~ and ~~crystallized,~~ and a ~~crystallographic data set was collected~~. ~~The crystals belonged~~ to the ~~monoclinic space group C2,~~ with ~~unit~~-~~cell parameters a = 79~~.2, ~~b = 69.9~~, ~~c = 57~~.~~9 A~~, ~~beta = 129.3 degrees , contained one monomer per asymmetric unit~~ and ~~diffracted to a resolution~~ of 1.~~98 A~~.	+	Although the oxidative condensation of two thiosulfate anions to tetrathionate constitutes a well-documented and significant part of the natural sulfur cycle little is known about the enzymes catalyzing this reaction. In the purple sulfur bacterium Allochromatium vinosum, the reaction is catalyzed by the periplasmic diheme c-type cytochrome thiosulfate dehydrogenase (TsdA). Here, we report the crystal structure of the 'as-isolated' form of A. vinosum TsdA to 1.98 A resolution, and those of several redox states of the enzyme to different resolutions. The protein contains two typical class I c-type cytochrome domains wrapped around two hemes axially coordinated by His-53/Cys-96 and His-164/Lys-208. These domains are very similar suggesting a gene duplication event during evolution. A ligand switch from Lys-208 to Met-209 is observed upon reduction of the enzyme. Cys-96 is an essential residue for catalysis with the specific activity of the enzyme being completely abolished in several TsdA-Cys-96 variants. TsdA-K208N, K208G and M209G variants were catalytically active in thiosulfate oxidation as well as in tetrathionate reduction, pointing to heme 2 as the electron exit point. In this study, we provide spectroscopic and structural evidence that the TsdA reaction cycle involves the transient presence of heme 1 in the high-spin state caused by movement of the Sgamma atom of Cys-96 out of the iron coordination sphere. Based on the presented data, we draw important conclusions about the enzyme and propose a possible reaction mechanism for TsdA.

-	~~Production, crystallization and preliminary crystallographic analysis of~~ Allochromatium vinosum ~~thiosulfate dehydrogenase TsdA, an unusual acidophilic c-type cytochrome~~.,Brito JA~~, Gutierres A~~, Denkmann K, ~~Dahl C~~, Archer M ~~Acta Crystallogr F Struct~~ Biol ~~Commun~~. ~~2014 Oct;70(Pt 10):1424-7~~. ~~doi~~:~~, 10~~.~~1107/S2053230X14019384~~. ~~Epub 2014 Sep 25~~. PMID:~~25286955~~<ref>PMID:~~25286955~~</ref>	+	Thiosulfate Dehydrogenase (TsdA) from Allochromatium vinosum: Structural and Functional Insights into Thiosulfate Oxidation.,Brito JA, Denkmann K, Pereira IA, Archer M, Dahl C J Biol Chem. 2015 Feb 11. pii: jbc.M114.623397. PMID:25673691<ref>PMID:25673691</ref>

	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>

OCA at 12:55, 18 February 2015

OCA — Wed, 18 Feb 2015 12:55:17 GMT

←Older revision		Revision as of 12:55, 18 February 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum - dithionite soak==
		+	<StructureSection load='4wq9' size='340' side='right' caption='[[4wq9]], [[Resolution\|resolution]] 1.47Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4wq9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WQ9 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wq7\|4wq7]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </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=4wq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wq9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wq9 RCSB], [http://www.ebi.ac.uk/pdbsum/4wq9 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TSDA_ALLVD TSDA_ALLVD]] Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.<ref>PMID:16995898</ref> <ref>PMID:22779704</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The ability to perform the very simple oxidation of two molecules of thiosulfate to tetrathionate is widespread among prokaryotes. Despite the prevalent occurrence of tetrathionate formation and its well documented significance within the sulfur cycle, little is known about the enzymes that catalyze the oxidative condensation of two thiosulfate anions. To fill this gap, the thiosulfate dehydrogenase (TsdA) enzyme from the purple sulfur bacterium Allochromatium vinosum was recombinantly expressed in Escherichia coli, purified and crystallized, and a crystallographic data set was collected. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 79.2, b = 69.9, c = 57.9 A, beta = 129.3 degrees , contained one monomer per asymmetric unit and diffracted to a resolution of 1.98 A.

-	~~The entry 4wq9 is ON HOLD until Paper Publication~~	+	Production, crystallization and preliminary crystallographic analysis of Allochromatium vinosum thiosulfate dehydrogenase TsdA, an unusual acidophilic c-type cytochrome.,Brito JA, Gutierres A, Denkmann K, Dahl C, Archer M Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1424-7. doi:, 10.1107/S2053230X14019384. Epub 2014 Sep 25. PMID:25286955<ref>PMID:25286955</ref>

-	~~Authors: Brito~~, J.A.~~, Denkmann, K., Pereira, I.A.C., Dahl, C., Archer, M~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: Thiosulfate dehydrogenase ~~(TsdA) from Allochromatium vinosum -dithionite soak~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
-	[[Category: ~~Pereira~~, I.A.C]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Thiosulfate dehydrogenase]]
		+	[[Category: Archer, M]]
		+	[[Category: Brito, J A]]
		+	[[Category: Dahl, C]]
	[[Category: Denkmann, K]]		[[Category: Denkmann, K]]
-	[[Category: ~~Dahl~~, C]]	+	[[Category: Pereira, I A.C]]
-	[[Category: ~~Archer, M~~]]	+	[[Category: C-type cytochrome]]
-	[[Category: ~~Brito, J.A~~]]	+	[[Category: Oxidoreductase]]
		+	[[Category: Tetrathionate]]
		+	[[Category: Tsda]]

OCA at 19:51, 24 December 2014

OCA — Wed, 24 Dec 2014 19:51:55 GMT

←Older revision		Revision as of 19:51, 24 December 2014
Line 6:		Line 6:

	Description: Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum -dithionite soak		Description: Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum -dithionite soak
		+	[[Category: Unreleased Structures]]
		+	[[Category: Pereira, I.A.C]]
		+	[[Category: Denkmann, K]]
		+	[[Category: Dahl, C]]
		+	[[Category: Archer, M]]
		+	[[Category: Brito, J.A]]

OCA at 09:52, 24 December 2014

OCA — Wed, 24 Dec 2014 09:52:05 GMT

←Older revision		Revision as of 09:52, 24 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4wq9 is ON HOLD	+	The entry 4wq9 is ON HOLD until Paper Publication

	Authors: Brito, J.A., Denkmann, K., Pereira, I.A.C., Dahl, C., Archer, M.		Authors: Brito, J.A., Denkmann, K., Pereira, I.A.C., Dahl, C., Archer, M.

	Description: Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum -dithionite soak		Description: Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum -dithionite soak

OCA: Protected "4wq9" [edit=sysop:move=sysop]

OCA — Wed, 29 Oct 2014 10:35:08 GMT

Protected "4wq9" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:35, 29 October 2014

OCA: New page: '''Unreleased structure''' The entry 4wq9 is ON HOLD Authors: Brito, J.A., Denkmann, K., Pereira, I.A.C., Dahl, C., Archer, M. Description: Thiosulfate dehydrogenase (TsdA) from Alloch...

OCA — Wed, 29 Oct 2014 10:35:06 GMT

New page: '''Unreleased structure''' The entry 4wq9 is ON HOLD Authors: Brito, J.A., Denkmann, K., Pereira, I.A.C., Dahl, C., Archer, M. Description: Thiosulfate dehydrogenase (TsdA) from Alloch...

New page

'''Unreleased structure'''

The entry 4wq9 is ON HOLD

Authors: Brito, J.A., Denkmann, K., Pereira, I.A.C., Dahl, C., Archer, M.

Description: Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum -dithionite soak