2myt: Difference between revisions
New page: '''Unreleased structure''' The entry 2myt is ON HOLD until Paper Publication Authors: Jin, C., Yu, C., Hu, C., Hu, Y. Description: An arsenate reductase in the intermediate state [[Cat... |
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==An arsenate reductase in the intermediate state== | |||
<StructureSection load='2myt' size='340' side='right'caption='[[2myt]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2myt]] 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=2MYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MYT FirstGlance]. <br> | |||
</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2myt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myt OCA], [https://pdbe.org/2myt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2myt RCSB], [https://www.ebi.ac.uk/pdbsum/2myt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2myt 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> | |||
<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> | |||
[[Category: | </div> | ||
[[Category: Hu | <div class="pdbe-citations 2myt" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Jin | ==See Also== | ||
[[Category: | *[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] | |||
[[Category: Hu C]] | |||
[[Category: Hu Y]] | |||
[[Category: Jin C]] | |||
[[Category: Yu C]] | |||
Latest revision as of 11:19, 30 October 2024
An arsenate reductase in the intermediate stateAn arsenate reductase in the intermediate state
Structural highlights
FunctionARSC_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 PubMedEvolution 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. See AlsoReferences
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