2myt: Difference between revisions
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==An arsenate reductase in the intermediate state== | ==An arsenate reductase in the intermediate state== | ||
<StructureSection load='2myt' size='340' side='right' caption='[[2myt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2myt' size='340' side='right' caption='[[2myt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2myt]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYT FirstGlance]. <br> | <table><tr><td colspan='2'>[[2myt]] 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=2MYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYT FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2myn|2myn]], [[2myp|2myp]], [[2myu|2myu]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2myn|2myn]], [[2myp|2myp]], [[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=2myt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myt OCA], [http://pdbe.org/2myt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myt RCSB], [http://www.ebi.ac.uk/pdbsum/2myt 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=2myt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myt OCA], [http://pdbe.org/2myt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2myt RCSB], [http://www.ebi.ac.uk/pdbsum/2myt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2myt ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Syny3]] | |||
[[Category: Hu, C]] | [[Category: Hu, C]] | ||
[[Category: Hu, Y]] | [[Category: Hu, Y]] | ||
Revision as of 18:57, 16 November 2017
An arsenate reductase in the intermediate stateAn arsenate reductase in the intermediate state
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 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. References
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