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| | ==An arsenate reductase in the intermediate state== | | ==An arsenate reductase in the intermediate state== |
| - | <StructureSection load='2l19' size='340' side='right'caption='[[2l19]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l19' size='340' side='right'caption='[[2l19]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l19]] 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=2L19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L19 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l19]] 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=2L19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L19 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;'>[[2l17|2l17]], [[2l18|2l18]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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>
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| - | <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>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l19 OCA], [https://pdbe.org/2l19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l19 RCSB], [https://www.ebi.ac.uk/pdbsum/2l19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l19 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=2l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l19 OCA], [https://pdbe.org/2l19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l19 RCSB], [https://www.ebi.ac.uk/pdbsum/2l19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l19 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]] | + | |
| Structural highlights
Function
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.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li R, Haile JD, Kennelly PJ. An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics. J Bacteriol. 2003 Dec;185(23):6780-9. PMID:14617642
- ↑ Lopez-Maury L, Sanchez-Riego AM, Reyes JC, Florencio FJ. The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803. J Bacteriol. 2009 Jun;191(11):3534-43. doi: 10.1128/JB.01798-08. Epub 2009 Mar, 20. PMID:19304854 doi:http://dx.doi.org/10.1128/JB.01798-08
- ↑ Kim SG, Chung JS, Sutton RB, Lee JS, Lopez-Maury L, Lee SY, Florencio FJ, Lin T, Zabet-Moghaddam M, Wood MJ, Nayak K, Madem V, Tripathy JN, Kim SK, Knaff DB. Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803. Biochim Biophys Acta. 2012 Feb;1824(2):392-403. Epub 2011 Oct 29. PMID:22155275 doi:10.1016/j.bbapap.2011.10.012
- ↑ Yu C, Xia B, Jin C. (1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803. Biomol NMR Assign. 2011 Apr;5(1):85-7. Epub 2010 Oct 20. PMID:20960080 doi:10.1007/s12104-010-9273-2
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