1lju

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(New page: 200px<br /><applet load="1lju" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lju, resolution 1.4&Aring;" /> '''X-RAY STRUCTURE OF C1...)
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[[Image:1lju.jpg|left|200px]]<br /><applet load="1lju" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lju, resolution 1.4&Aring;" />
 
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'''X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE'''<br />
 
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==Overview==
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==X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE==
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The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate, reduction, involving its P-loop structural motif and three redox active, cysteines, has been unraveled. All essential intermediates are visualized, with x-ray crystallography, and NMR is used to map dynamic regions in a, key disulfide intermediate. Steady-state kinetics of ArsC mutants gives a, view of the crucial residues for catalysis. ArsC combines a, phosphatase-like nucleophilic displacement reaction with a unique, intramolecular disulfide bond cascade. Within this cascade, the formation, of a disulfide bond triggers a reversible "conformational switch" that, transfers the oxidative equivalents to the surface of the protein, while, releasing the reduced substrate.
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<StructureSection load='1lju' size='340' side='right'caption='[[1lju]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lju]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJU FirstGlance]. <br>
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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]] 1.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSR:S-ARSONOCYSTEINE'>CSR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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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=1lju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lju OCA], [https://pdbe.org/1lju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lju RCSB], [https://www.ebi.ac.uk/pdbsum/1lju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lju ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARSC_STAAU ARSC_STAAU] Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances.[HAMAP-Rule:MF_01624]
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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/lj/1lju_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1lju ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate reduction, involving its P-loop structural motif and three redox active cysteines, has been unraveled. All essential intermediates are visualized with x-ray crystallography, and NMR is used to map dynamic regions in a key disulfide intermediate. Steady-state kinetics of ArsC mutants gives a view of the crucial residues for catalysis. ArsC combines a phosphatase-like nucleophilic displacement reaction with a unique intramolecular disulfide bond cascade. Within this cascade, the formation of a disulfide bond triggers a reversible "conformational switch" that transfers the oxidative equivalents to the surface of the protein, while releasing the reduced substrate.
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==About this Structure==
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All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.,Messens J, Martins JC, Van Belle K, Brosens E, Desmyter A, De Gieter M, Wieruszeski JM, Willem R, Wyns L, Zegers I Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8506-11. Epub 2002 Jun 18. PMID:12072565<ref>PMID:12072565</ref>
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1LJU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LJU OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade., Messens J, Martins JC, Van Belle K, Brosens E, Desmyter A, De Gieter M, Wieruszeski JM, Willem R, Wyns L, Zegers I, Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8506-11. Epub 2002 Jun 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12072565 12072565]
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</div>
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[[Category: Arsenate reductase (glutaredoxin)]]
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<div class="pdbe-citations 1lju" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
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[[Category: Martins, J.C.]]
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[[Category: Messens, J.]]
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[[Category: Willem, R.]]
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[[Category: Wyns, L.]]
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[[Category: Zegers, I.]]
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[[Category: K]]
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[[Category: p-loop]]
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[[Category: ptpase i fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:36:36 2007''
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==See Also==
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*[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Staphylococcus aureus]]
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[[Category: Martins JC]]
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[[Category: Messens J]]
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[[Category: Willem R]]
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[[Category: Wyns L]]
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[[Category: Zegers I]]

Current revision

X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE

PDB ID 1lju

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