1sd8: Difference between revisions

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<StructureSection load='1sd8' size='340' side='right'caption='[[1sd8]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
<StructureSection load='1sd8' size='340' side='right'caption='[[1sd8]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1sd8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SD8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1sd8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SD8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s3c|1s3c]], [[1s3d|1s3d]], [[1sd9|1sd9]], [[1sjz|1sjz]], [[1sk0|1sk0]], [[1sk1|1sk1]], [[1sk2|1sk2]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sd8 OCA], [https://pdbe.org/1sd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sd8 RCSB], [https://www.ebi.ac.uk/pdbsum/1sd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sd8 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=1sd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sd8 OCA], [https://pdbe.org/1sd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sd8 RCSB], [https://www.ebi.ac.uk/pdbsum/1sd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sd8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ARSC1_ECOLX ARSC1_ECOLX]] Reduction of arsenate [As(V)] to arsenite [As(III)]. This protein expands the substrate specificity of ArsAB pump which can extrude arsenite and antimonite to allow for arsenate pumping and resistance.  
[https://www.uniprot.org/uniprot/ARSC1_ECOLX ARSC1_ECOLX] Reduction of arsenate [As(V)] to arsenite [As(III)]. This protein expands the substrate specificity of ArsAB pump which can extrude arsenite and antimonite to allow for arsenate pumping and resistance.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sd8 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sd8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arsenic is a ubiquitous environmental toxic metal. Consequently, organisms detoxify arsenate by reduction to arsenite, which is then excreted or sequestered. The ArsC arsenate reductase from Escherichia coli plasmid R773, the best characterized arsenic-modifying enzyme, has a catalytic cysteine, Cys 12, in the active site, surrounded by an arginine triad composed of Arg 60, Arg 94, and Arg 107. During the reaction cycle, the native enzyme forms a unique monohydroxyl Cys 12-thiol-arsenite adduct that contains a positive charge on the arsenic. We hypothesized previously that this unstable intermediate allows for rapid dissociation of the product arsenite. In this study, the role of Arg 60 in product formation was evaluated by mutagenesis. A total of eight new structures of ArsC were determined at resolutions between 1.3 A and 1.8 A, with R(free) values between 0.18 and 0.25. The crystal structures of R60K and R60A ArsC equilibrated with the product arsenite revealed a covalently bound Cys 12-thiol-dihydroxyarsenite without a charge on the arsenic atom. We propose that this intermediate is more stable than the monohydroxyarsenite intermediate of the native enzyme, resulting in slow release of product and, consequently, loss of activity.
Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product.,DeMel S, Shi J, Martin P, Rosen BP, Edwards BF Protein Sci. 2004 Sep;13(9):2330-40. Epub 2004 Aug 4. PMID:15295115<ref>PMID:15295115</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1sd8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]]
*[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: DeMel, S]]
[[Category: DeMel S]]
[[Category: Edwards, B F]]
[[Category: Edwards BF]]
[[Category: Arsc]]
[[Category: Arsenate]]
[[Category: Arsenite]]
[[Category: Oxidoreductase]]
[[Category: Reductase]]

Latest revision as of 11:29, 14 February 2024

ARSENATE REDUCTASE R60K MUTANT FROM E. COLIARSENATE REDUCTASE R60K MUTANT FROM E. COLI

Structural highlights

1sd8 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.59Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARSC1_ECOLX Reduction of arsenate [As(V)] to arsenite [As(III)]. This protein expands the substrate specificity of ArsAB pump which can extrude arsenite and antimonite to allow for arsenate pumping and resistance.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1sd8, resolution 1.59Å

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