1sjz: Difference between revisions

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-{{Seed}}
-[[Image:1sjz.png|left|200px]]
-<!--
+==ARSENATE REDUCTASE R60K MUTANT +0.4M ARSENITE FROM E. COLI==
-The line below this paragraph, containing "STRUCTURE_1sjz", creates the "Structure Box" on the page.
+<StructureSection load='1sjz' size='340' side='right'caption='[[1sjz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1sjz]] 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=1SJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SJZ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=CZ2:S-(DIHYDROXYARSINO)CYSTEINE'>CZ2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TAS:TRIHYDROXYARSENITE(III)'>TAS</scene></td></tr>
-{{STRUCTURE_1sjz|  PDB=1sjz  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjz OCA], [https://pdbe.org/1sjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sjz RCSB], [https://www.ebi.ac.uk/pdbsum/1sjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sjz ProSAT]</span></td></tr>
+</table>
+== 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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sj/1sjz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1sjz ConSurf].
+<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.
-===ARSENATE REDUCTASE R60K MUTANT +0.4M ARSENITE FROM E. COLI===
+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 1sjz" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15295115}}, adds the Publication Abstract to the page
+*[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15295115 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15295115}}
+__TOC__
+</StructureSection>
-==About this Structure==
-SJZ is a 1 chain 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=1SJZ OCA].
-==Reference==
-<ref group="xtra">PMID:15295115</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Demel, S.]]
+[[Category: Large Structures]]
-[[Category: Edwards, B F.]]
+[[Category: Demel S]]
-[[Category: Arsc]]
+[[Category: Edwards BF]]
-[[Category: Arsenate]]
-[[Category: Arsenite]]
-[[Category: Reductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:52:52 2009''