2myp: Difference between revisions

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== 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>  
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2myp" style="background-color:#fffaf0;"></div>


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

Latest revision as of 07:03, 1 May 2024

An arsenate reductase in the phosphate binding state

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