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New page: left|200px<br /><applet load="1ii0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ii0, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1ii0.gif|left|200px]]<br /><applet load="1ii0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ii0, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE==
Structures of ArsA with ATP, AMP-PNP, or ADP.AlF(3) bound at the A2, nucleotide binding site were determined. Binding of different nucleotides, modifies the coordination sphere of Mg(2+). In particular, the changes, elicited by ADP.AlF(3) provide insights into the mechanism of ATP, hydrolysis. In-line attack by water onto the gamma-phosphate of ATP would, be followed first by formation of a trigonal intermediate and then by, breaking of the scissile bond between the beta- and gamma-phosphates., Motions of amino acid side chains at the A2 nucleotide binding site during, ATP binding and hydrolysis propagate at a distance, producing, conformational changes in four different regions of the protein, corresponding to helices H4-H5, helices H9-H10, helices H13-H15, and to, the S1-H2-S2 region. These elements are extensions of, respectively, the, Switch I and Switch II regions, the A-loop (a small loop near the, nucleotide adenine moiety), and the P-loop. Based on the observed, conformational changes, it is proposed that ArsA functions as a, reciprocating engine that hydrolyzes 2 mol of ATP per each cycle of ion, translocation across the membrane.
<StructureSection load='1ii0' size='340' side='right'caption='[[1ii0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ii0]] is a 2 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=1II0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1II0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAS:TRIHYDROXYARSENITE(III)'>TAS</scene></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=1ii0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii0 OCA], [https://pdbe.org/1ii0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ii0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ii0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ii0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARSA1_ECOLX ARSA1_ECOLX] Anion-transporting ATPase. Catalyzes the extrusion of the oxyanions arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents.
== 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/ii/1ii0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ii0 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1II0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CD, CL, MG, ADP, ATP and TAS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arsenite-transporting_ATPase Arsenite-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.16 3.6.3.16] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1II0 OCA].
*[[ATPase 3D structures|ATPase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation., Zhou T, Radaev S, Rosen BP, Gatti DL, J Biol Chem. 2001 Aug 10;276(32):30414-22. Epub 2001 Jun 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11395509 11395509]
[[Category: Arsenite-transporting ATPase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Gatti, D.L.]]
[[Category: Gatti DL]]
[[Category: Radaev, S.]]
[[Category: Radaev S]]
[[Category: Rosen, B.P.]]
[[Category: Rosen BP]]
[[Category: Zhou, T.]]
[[Category: Zhou T]]
[[Category: ADP]]
[[Category: ATP]]
[[Category: CD]]
[[Category: CL]]
[[Category: MG]]
[[Category: TAS]]
[[Category: arsa atpase]]
[[Category: atp]]
[[Category: atp binding site]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:24:48 2007''

Latest revision as of 07:35, 7 February 2024

CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE

1ii0, resolution 2.40Å

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