2l17 - Revision history

OCA at 06:51, 1 May 2024

OCA — Wed, 01 May 2024 06:51:25 GMT

←Older revision		Revision as of 06:51, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L17 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L17 FirstGlance]. <br>
-	</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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [https://pdbe.org/2l17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [https://www.ebi.ac.uk/pdbsum/2l17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l17 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [https://pdbe.org/2l17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [https://www.ebi.ac.uk/pdbsum/2l17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l17 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>		[https://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Arsenate reductases (ArsC) are a group of enzymes that play essential roles in biological arsenic detoxification pathways by catalyzing the intracellular reduction of arsenate to arsenite, which is subsequently extruded from the cells by specific transport systems. The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. Herein we report the chemical shift assignments of (1)H, (13)C and (15)N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.
-
-	(1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803.,Yu C, Xia B, Jin C Biomol NMR Assign. 2011 Apr;5(1):85-7. Epub 2010 Oct 20. PMID:20960080<ref>PMID:20960080</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2l17" style="background-color:#fffaf0;"></div>

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

OCA at 08:12, 18 January 2023

OCA — Wed, 18 Jan 2023 08:12:15 GMT

←Older revision		Revision as of 08:12, 18 January 2023
Line 1:		Line 1:

	==An arsenate reductase in the reduced state==		==An arsenate reductase in the reduced state==
-	<StructureSection load='2l17' size='340' side='right'caption='[[2l17~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2l17' size='340' side='right'caption='[[2l17]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Aphanocapsa_sp~~.~~_(strain_n-1) Aphanocapsa~~ sp. ~~(strain n-1)~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L17 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L17 FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2l18\|2l18]], [[2l19\|2l19]]</div></td></tr>~~	+	</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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [https://pdbe.org/2l17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [https://www.ebi.ac.uk/pdbsum/2l17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l17 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [https://pdbe.org/2l17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [https://www.ebi.ac.uk/pdbsum/2l17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l17 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>	+	[https://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Jin, C~~]]	+	[[Category: Synechocystis sp. PCC 6803]]
-	[[Category: ~~Xia, B]]~~	+	[[Category: Jin C]]
-	~~[[Category: Yu,~~ C]]	+	[[Category: Xia B]]
-	[[Category: ~~Alpha/beta sandwich~~]]	+	[[Category: Yu C]]
-	[[Category: ~~Oxidoreductase~~]]	+

OCA at 07:34, 14 April 2021

OCA — Wed, 14 Apr 2021 07:34:46 GMT

←Older revision		Revision as of 07:34, 14 April 2021
Line 1:		Line 1:

	==An arsenate reductase in the reduced state==		==An arsenate reductase in the reduced state==
-	<StructureSection load='2l17' size='340' side='right' caption='[[2l17]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2l17' size='340' side='right'caption='[[2l17]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2L17 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L17 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2l18\|2l18]], [[2l19\|2l19]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2l18\|2l18]], [[2l19\|2l19]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [~~http~~://pdbe.org/2l17 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2l17 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2l17 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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [https://pdbe.org/2l17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [https://www.ebi.ac.uk/pdbsum/2l17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l17 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>	+	[[https://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:

	==See Also==		==See Also==
-	*[[Arsenate reductase\|Arsenate reductase]]	+	*[[Arsenate reductase 3D structures\|Arsenate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Jin, C]]		[[Category: Jin, C]]
	[[Category: Xia, B]]		[[Category: Xia, B]]

OCA at 08:28, 25 July 2018

OCA — Wed, 25 Jul 2018 08:28:27 GMT

←Older revision		Revision as of 08:28, 25 July 2018
Line 1:		Line 1:
		+
	==An arsenate reductase in the reduced state==		==An arsenate reductase in the reduced state==
	<StructureSection load='2l17' size='340' side='right' caption='[[2l17]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2l17' size='340' side='right' caption='[[2l17]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://pdbe.org/2l17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://pdbe.org/2l17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l17 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 13:17, 11 September 2015

OCA — Fri, 11 Sep 2015 13:17:42 GMT

←Older revision		Revision as of 13:17, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2l17' size='340' side='right' caption='[[2l17]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2l17' size='340' side='right' caption='[[2l17]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Synechocystis Synechocystis~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L17 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L17 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2l18\|2l18]], [[2l19\|2l19]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2l18\|2l18]], [[2l19\|2l19]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~1142 Synechocystis~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://pdbe.org/2l17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~P74313_SYNY3 P74313_SYNY3~~]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>	+	[[http://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_SYNY3]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 18:
	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 2l17" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Synechocystis]]
	[[Category: Jin, C]]		[[Category: Jin, C]]
	[[Category: Xia, B]]		[[Category: Xia, B]]

OCA at 16:57, 25 December 2014

OCA — Thu, 25 Dec 2014 16:57:31 GMT

←Older revision		Revision as of 16:57, 25 December 2014
Line 8:		Line 8:
	<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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/P74313_SYNY3 P74313_SYNY3]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 08:49, 26 November 2014

OCA — Wed, 26 Nov 2014 08:49:02 GMT

←Older revision		Revision as of 08:49, 26 November 2014
Line 1:		Line 1:
-	[[~~Image:~~2l17.~~png~~\|~~left~~\|~~200px~~]]	+	==An arsenate reductase in the reduced state==
		+	<StructureSection load='2l17' size='340' side='right' caption='[[2l17]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2l17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis Synechocystis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L17 FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2l18\|2l18]], [[2l19\|2l19]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1142 Synechocystis])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </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=2l17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l17 RCSB], [http://www.ebi.ac.uk/pdbsum/2l17 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Arsenate reductases (ArsC) are a group of enzymes that play essential roles in biological arsenic detoxification pathways by catalyzing the intracellular reduction of arsenate to arsenite, which is subsequently extruded from the cells by specific transport systems. The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. Herein we report the chemical shift assignments of (1)H, (13)C and (15)N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.

-	~~{{STRUCTURE_2l17\| PDB=2l17 \| SCENE= }}~~	+	(1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803.,Yu C, Xia B, Jin C Biomol NMR Assign. 2011 Apr;5(1):85-7. Epub 2010 Oct 20. PMID:20960080<ref>PMID:20960080</ref>

-	~~===An arsenate reductase in~~ the ~~reduced state===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_20960080}}~~	+	==See Also==
-		+	*[[Arsenate reductase\|Arsenate reductase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~2l17~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis Synechocystis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:020960080<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Synechocystis]]		[[Category: Synechocystis]]
-	[[Category: Jin, C.]]	+	[[Category: Jin, C]]
-	[[Category: Xia, B.]]	+	[[Category: Xia, B]]
-	[[Category: Yu, C.]]	+	[[Category: Yu, C]]
	[[Category: Alpha/beta sandwich]]		[[Category: Alpha/beta sandwich]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 14:36, 20 February 2013

OCA — Wed, 20 Feb 2013 14:36:16 GMT

←Older revision		Revision as of 14:36, 20 February 2013
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-	[[Image:2l17.~~jpg~~\|left\|200px]]	+	[[Image:2l17.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2l17\| PDB=2l17 \| SCENE= }}		{{STRUCTURE_2l17\| PDB=2l17 \| SCENE= }}

	===An arsenate reductase in the reduced state===		===An arsenate reductase in the reduced state===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20960080}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20960080 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_20960080}}		{{ABSTRACT_PUBMED_20960080}}

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	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20960080~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020960080</ref><references group="xtra"/>
	[[Category: Synechocystis]]		[[Category: Synechocystis]]
	[[Category: Jin, C.]]		[[Category: Jin, C.]]
	[[Category: Xia, B.]]		[[Category: Xia, B.]]
	[[Category: Yu, C.]]		[[Category: Yu, C.]]
		+	[[Category: Alpha/beta sandwich]]
		+	[[Category: Oxidoreductase]]

OCA: Protected "2l17" [edit=sysop:move=sysop]

OCA — Wed, 13 Apr 2011 05:13:01 GMT

Protected "2l17" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:13, 13 April 2011

OCA at 05:12, 13 April 2011

OCA — Wed, 13 Apr 2011 05:12:59 GMT

←Older revision		Revision as of 05:12, 13 April 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:2l17.jpg\|left\|200px]]

-	The ~~entry 2l17~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2l17", 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_2l17\| PDB=2l17 \| SCENE= }}

-	~~Authors: Yu, C., Xia, B., Jin, C.~~	+	===An arsenate reductase in the reduced state===

-	Description: An arsenate reductase in the reduced state

-	~~''Page seeded by~~ [http://oca.weizmann.ac.il/oca OCA ] ~~on Wed Aug 11 23~~:28:~~00 2010''~~	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20960080}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20960080 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20960080}}
		+
		+	==About this Structure==
		+	[[2l17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis Synechocystis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L17 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20960080</ref><references group="xtra"/>
		+	[[Category: Synechocystis]]
		+	[[Category: Jin, C.]]
		+	[[Category: Xia, B.]]
		+	[[Category: Yu, C.]]