View source for 1mwz


==Solution structure of the N-terminal domain of ZntA in the Zn(II)-form==
<StructureSection load='1mwz' size='340' side='right'caption='[[1mwz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mwz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1mwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwz OCA], [https://pdbe.org/1mwz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwz RCSB], [https://www.ebi.ac.uk/pdbsum/1mwz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ZNTA_ECOLI ZNTA_ECOLI] Confers resistance to zinc, cadmium and lead (PubMed:9405611, PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661). Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes (PubMed:9405611, PubMed:10660539, PubMed:17326661). Can also bind nickel, copper, cobalt and mercury (PubMed:10660539, PubMed:17326661).<ref>PMID:10660539</ref> <ref>PMID:17326661</ref> <ref>PMID:9364914</ref> <ref>PMID:9405611</ref> <ref>PMID:9830000</ref> 
== 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/mw/1mwz_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=1mwz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Zinc, a metal ion that functions in a wide variety of catalytic and structural sites in metalloproteins, is shown here to adopt a novel coordination environment in the Escherichia coli transport protein ZntA. The ZntA protein is a P-type ATPase that pumps zinc out of the cytoplasm and into the periplasm. It is physiologically selective for Zn(II) and functions with metalloregulatory proteins in the cell to keep the zinc quota within strict limits. Yet, the N-terminal cytoplasmic domain contains a region that is highly homologous to the yeast Cu(I) metallochaperone Atx1. To investigate how the structure of this region may influence its function, this fragment, containing residues 46-118, has been cloned out of the gene and overexpressed. We report here the solution structure of this fragment as determined by NMR. Both the apo and Zn(II)-ZntA(46-118) structures have been determined. It contains a previously unknown protein coordination site for zinc that includes two cysteine residues, Cys59 and Cys62, and a carboxylate residue, Asp58. The solvent accessibility of this site is also remarkably high, a feature that increasingly appears to be a characteristic of domains of heavy metal ion transport proteins. The participation of Asp58 in this ZntA metal ion binding site may play an important role in modulating the relative affinities and metal exchange rates for Zn(II)/Pb(II)/Cd(II) as compared with other P-type ATPases, which are selective for Cu(I) or Ag(I).

A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118).,Banci L, Bertini I, Ciofi-Baffoni S, Finney LA, Outten CE, O'Halloran TV J Mol Biol. 2002 Nov 8;323(5):883-97. PMID:12417201<ref>PMID:12417201</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1mwz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Banci L]]
[[Category: Bertini I]]
[[Category: Ciofi-Baffoni S]]
[[Category: Finney LA]]
[[Category: O'Halloran TV]]
[[Category: Outten CE]]