2myp - Revision history

OCA at 07:03, 1 May 2024

2024-05-01T07:03:07Z

←Older revision		Revision as of 07:03, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2myp]] 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=2MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2myp]] 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=2MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYP 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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [https://pdbe.org/2myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [https://www.ebi.ac.uk/pdbsum/2myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp 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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [https://pdbe.org/2myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [https://www.ebi.ac.uk/pdbsum/2myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp 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 ==
-	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 2myp" style="background-color:#fffaf0;"></div>

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

OCA at 08:11, 8 March 2023

2023-03-08T08:11:10Z

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

	==An arsenate reductase in the phosphate binding state==		==An arsenate reductase in the phosphate binding state==
-	<StructureSection load='2myp' size='340' side='right'caption='[[2myp~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2myp' size='340' side='right'caption='[[2myp]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2myp]] 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=2MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2myp]] 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=2MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYP 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]], [[2myt\|2myt]], [[2myu\|2myu]]</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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [https://pdbe.org/2myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [https://www.ebi.ac.uk/pdbsum/2myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp 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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [https://pdbe.org/2myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [https://www.ebi.ac.uk/pdbsum/2myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp 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: Yu, C]]	+	[[Category: Yu C]]
-	~~[[Category: Alpha/beta/alpha sandwich fold]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 15:23, 2 June 2021

2021-06-02T15:23:36Z

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

	==An arsenate reductase in the phosphate binding state==		==An arsenate reductase in the phosphate binding state==
-	<StructureSection load='2myp' size='340' side='right' caption='[[2myp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2myp' size='340' side='right'caption='[[2myp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2myp]] 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=2MYP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2MYP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2myp]] 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=2MYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYP FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myt\|2myt]], [[2myu\|2myu]]</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]], [[2myt\|2myt]], [[2myu\|2myu]]</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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [~~http~~://pdbe.org/2myp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2myp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp 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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [https://pdbe.org/2myp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [https://www.ebi.ac.uk/pdbsum/2myp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp 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 2myp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2myp" 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

2017-11-16T15:57:13Z

←Older revision		Revision as of 15:57, 16 November 2017
Line 1:		Line 1:
		+
	==An arsenate reductase in the phosphate binding state==		==An arsenate reductase in the phosphate binding state==
	<StructureSection load='2myp' size='340' side='right' caption='[[2myp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2myp' size='340' side='right' caption='[[2myp]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2myp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2myp]] 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=2MYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYP FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myt\|2myt]], [[2myu\|2myu]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myt\|2myt]], [[2myu\|2myu]]</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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [http://pdbe.org/2myp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [http://www.ebi.ac.uk/pdbsum/2myp 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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [http://pdbe.org/2myp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [http://www.ebi.ac.uk/pdbsum/2myp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2myp 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 07:26, 30 September 2015

2015-09-30T07:26:02Z

←Older revision		Revision as of 07:26, 30 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[2myp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2myp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYP FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myt\|2myt]], [[2myu\|2myu]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2myn\|2myn]], [[2myt\|2myt]], [[2myu\|2myu]]</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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [http://www.ebi.ac.uk/pdbsum/2myp 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=2myp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myp OCA], [http://pdbe.org/2myp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myp RCSB], [http://www.ebi.ac.uk/pdbsum/2myp 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 2myp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:08, 5 August 2015

2015-08-05T20:08:04Z

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

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

2015-02-12T06:48:17Z

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

←Older revision

Revision as of 06:48, 12 February 2015

OCA: New page: '''Unreleased structure''' The entry 2myp is ON HOLD until Paper Publication Authors: Jin, C., Yu, C., Hu, C., Hu, Y. Description: An arsenate reductase in the phosphate binding state ...

2015-02-12T06:48:16Z

New page: '''Unreleased structure''' The entry 2myp is ON HOLD until Paper Publication Authors: Jin, C., Yu, C., Hu, C., Hu, Y. Description: An arsenate reductase in the phosphate binding state ...

New page

'''Unreleased structure'''

The entry 2myp is ON HOLD until Paper Publication

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

Description: An arsenate reductase in the phosphate binding state
[[Category: Unreleased Structures]]
[[Category: Hu, Y]]
[[Category: Yu, C]]
[[Category: Jin, C]]
[[Category: Hu, C]]