2myu - Revision history

OCA at 08:11, 8 March 2023

OCA — Wed, 08 Mar 2023 08:11:14 GMT

←Older revision		Revision as of 08:11, 8 March 2023
Line 1:		Line 1:

	==An arsenate reductase in oxidized state==		==An arsenate reductase in oxidized state==
-	<StructureSection load='2myu' size='340' side='right'caption='[[2myu~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2myu' size='340' side='right'caption='[[2myu]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Syny3 Syny3~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYU 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;'>[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [https://pdbe.org/2myu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [https://www.ebi.ac.uk/pdbsum/2myu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myu 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=1111708 SYNY3])</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [https://pdbe.org/2myu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [https://www.ebi.ac.uk/pdbsum/2myu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myu 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 ==
Line 27:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Syny3~~]]	+	[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
-	[[Category: Hu, C]]	+	[[Category: Hu C]]
-	[[Category: Hu, Y]]	+	[[Category: Hu Y]]
-	[[Category: Jin, C]]	+	[[Category: Jin C]]
-	~~[[Category: Alpha/beta/alpha sandwich fold]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 15:23, 2 June 2021

OCA — Wed, 02 Jun 2021 15:23:39 GMT

←Older revision		Revision as of 15:23, 2 June 2021
Line 1:		Line 1:

	==An arsenate reductase in oxidized state==		==An arsenate reductase in oxidized state==
-	<StructureSection load='2myu' size='340' side='right' caption='[[2myu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2myu' size='340' side='right'caption='[[2myu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Syny3 Syny3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2MYU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Syny3 Syny3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYU FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</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;'>[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</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=1111708 SYNY3])</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=1111708 SYNY3])</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [~~http~~://pdbe.org/2myu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2myu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2myu 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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [https://pdbe.org/2myu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [https://www.ebi.ac.uk/pdbsum/2myu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myu 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 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 2myu" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2myu" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Arsenate reductase 3D structures\|Arsenate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Syny3]]		[[Category: Syny3]]
	[[Category: Hu, C]]		[[Category: Hu, C]]

OCA at 15:57, 16 November 2017

OCA — Thu, 16 Nov 2017 15:57:28 GMT

←Older revision		Revision as of 15:57, 16 November 2017
Line 1:		Line 1:
		+
	==An arsenate reductase in oxidized state==		==An arsenate reductase in oxidized state==
	<StructureSection load='2myu' size='340' side='right' caption='[[2myu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2myu' size='340' side='right' caption='[[2myu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYU FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [http://pdbe.org/2myu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [http://www.ebi.ac.uk/pdbsum/2myu PDBsum]</span></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=1111708 SYNY3])</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [http://pdbe.org/2myu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [http://www.ebi.ac.uk/pdbsum/2myu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2myu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Syny3]]
	[[Category: Hu, C]]		[[Category: Hu, C]]
	[[Category: Hu, Y]]		[[Category: Hu, Y]]

OCA at 07:11, 30 September 2015

OCA — Wed, 30 Sep 2015 07:11:37 GMT

←Older revision		Revision as of 07:11, 30 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYU FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [http://www.ebi.ac.uk/pdbsum/2myu 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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [http://pdbe.org/2myu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [http://www.ebi.ac.uk/pdbsum/2myu PDBsum]</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>		[[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;">
		+	== Publication Abstract from PubMed ==
		+	Evolution of enzymes plays a crucial role in obtaining new biological functions for all life forms. Arsenate reductases (ArsC) are several families of arsenic detoxification enzymes that reduce arsenate to arsenite, which can subsequently be extruded from cells by specific transporters. Among these, the Synechocystis ArsC (SynArsC) is structurally homologous to the well characterized thioredoxin (Trx)-coupled ArsC family but requires the glutaredoxin (Grx) system for its reactivation, therefore classified as a unique Trx/Grx-hybrid family. The detailed catalytic mechanism of SynArsC is unclear and how the "hybrid" mechanism evolved remains enigmatic. Herein, we report the molecular mechanism of SynArsC by biochemical and structural studies. Our work demonstrates that arsenate reduction is carried out via an intramolecular thiol-disulfide cascade similar to the Trx-coupled family, whereas the enzyme reactivation step is diverted to the coupling of the glutathione-Grx pathway due to the local structural difference. The current results support the hypothesis that SynArsC is likely a molecular fossil representing an intermediate stage during the evolution of the Trx-coupled ArsC family from the low molecular weight protein phosphotyrosine phosphatase (LMW-PTPase) family.
		+
		+	A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.,Hu C, Yu C, Liu Y, Hou X, Liu X, Hu Y, Jin C J Biol Chem. 2015 Sep 4;290(36):22262-73. doi: 10.1074/jbc.M115.659896. Epub 2015, Jul 29. PMID:26224634<ref>PMID:26224634</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 2myu" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:08, 5 August 2015

OCA — Wed, 05 Aug 2015 20:08:19 GMT

←Older revision		Revision as of 20:08, 5 August 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==An arsenate reductase in oxidized state==
-		+	<StructureSection load='2myu' size='340' side='right' caption='[[2myu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~The entry~~ 2myu is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2myu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYU FirstGlance]. <br>
-	~~Authors~~: ~~Jin~~, C., ~~Hu, C~~., ~~Hu, Y~~.	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myp\|2myp]], [[2myt\|2myt]]</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [http://www.ebi.ac.uk/pdbsum/2myu PDBsum]</span></td></tr>
-	~~Description~~: An arsenate ~~reductase~~ in ~~oxidized state~~	+	</table>
-	[[Category: ~~Unreleased Structures~~]]	+	== 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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hu, C]]
	[[Category: Hu, Y]]		[[Category: Hu, Y]]
	[[Category: Jin, C]]		[[Category: Jin, C]]
-	[[Category: ~~Hu, C~~]]	+	[[Category: Alpha/beta/alpha sandwich fold]]
		+	[[Category: Oxidoreductase]]

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

OCA — Thu, 12 Feb 2015 06:48:27 GMT

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

←Older revision

Revision as of 06:48, 12 February 2015

OCA: New page: '''Unreleased structure''' The entry 2myu is ON HOLD until Paper Publication Authors: Jin, C., Hu, C., Hu, Y. Description: An arsenate reductase in oxidized state [[Category: Unrelease...

OCA — Thu, 12 Feb 2015 06:48:26 GMT

New page: '''Unreleased structure''' The entry 2myu is ON HOLD until Paper Publication Authors: Jin, C., Hu, C., Hu, Y. Description: An arsenate reductase in oxidized state [[Category: Unrelease...

New page

'''Unreleased structure'''

The entry 2myu is ON HOLD until Paper Publication

Authors: Jin, C., Hu, C., Hu, Y.

Description: An arsenate reductase in oxidized state
[[Category: Unreleased Structures]]
[[Category: Hu, Y]]
[[Category: Jin, C]]
[[Category: Hu, C]]