2myp: Difference between revisions

Revision as of 08:11, 8 March 2023

An arsenate reductase in the phosphate binding state

Structural highlights

2myp is a 1 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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:https://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
↑ Hu C, Yu C, Liu Y, Hou X, Liu X, Hu Y, Jin C. A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction. J Biol Chem. 2015 Sep 4;290(36):22262-73. doi: 10.1074/jbc.M115.659896. Epub 2015, Jul 29. PMID:26224634 doi:https://dx.doi.org/10.1074/jbc.M115.659896

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OCA

[1] 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

[2] 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:https://dx.doi.org/10.1128/JB.01798-08

[3] 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

[4] Hu C, Yu C, Liu Y, Hou X, Liu X, Hu Y, Jin C. A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction. J Biol Chem. 2015 Sep 4;290(36):22262-73. doi: 10.1074/jbc.M115.659896. Epub 2015, Jul 29. PMID:26224634 doi:https://dx.doi.org/10.1074/jbc.M115.659896

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
 ==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 ==
-<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>
 == 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 ==
@@ Line 27: / Line 25: @@
 </StructureSection>
 [[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]]

2myp: Difference between revisions

Revision as of 08:11, 8 March 2023

An arsenate reductase in the phosphate binding state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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