1s3c

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[[Image:1s3c.gif|left|200px]]
 
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{{Structure
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==ARSENATE REDUCTASE C12S MUTANT FROM E. COLI==
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|PDB= 1s3c |SIZE=350|CAPTION= <scene name='initialview01'>1s3c</scene>, resolution 1.25&Aring;
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<StructureSection load='1s3c' size='340' side='right'caption='[[1s3c]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CS:CESIUM ION'>CS</scene>
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<table><tr><td colspan='2'>[[1s3c]] 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=1S3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S3C FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
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|GENE=
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<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>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3c OCA], [https://pdbe.org/1s3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s3c RCSB], [https://www.ebi.ac.uk/pdbsum/1s3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s3c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s3/1s3c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1s3c ConSurf].
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<div style="clear:both"></div>
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'''ARSENATE REDUCTASE C12S MUTANT FROM E. COLI'''
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==See Also==
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*[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1S3C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3C OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15295115 15295115]
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[[Category: Arsenate reductase (glutaredoxin)]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: DeMel, S.]]
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[[Category: DeMel S]]
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[[Category: Edwards, B F.]]
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[[Category: Edwards BF]]
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[[Category: CS]]
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[[Category: SO4]]
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[[Category: arsc]]
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[[Category: arsenate]]
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[[Category: arsenite]]
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[[Category: reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:59:52 2008''
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Current revision

ARSENATE REDUCTASE C12S MUTANT FROM E. COLI

PDB ID 1s3c

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