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New page: left|200px<br /><applet load="1co4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1co4" /> '''SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVE...
 
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[[Image:1co4.gif|left|200px]]<br /><applet load="1co4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1co4" />
'''SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS'''<br />


==Overview==
==SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS==
The three dimensional structure of the N-terminal domain (residues 1-42), of the copper-responsive transcription factor Amtl from Candida glabrata, has been determined by two-dimensional 1H-correlated nuclear magnetic, resonance (NMR) methods. The domain contains an array of zinc-binding, residues (Cys-X2-Cys-X8-Cys-X-His) that is conserved among a family of, Cu-responsive transcription factors. The structure is unlike those of, previously characterized zinc finger motifs, and consists of a, three-stranded antiparallel beta-sheet with two short helical segments, that project from one end of the beta-sheet. Conserved residues at, positions 16, 18 and 19 form a basic patch that may be important for DNA, binding.
<StructureSection load='1co4' size='340' side='right'caption='[[1co4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1co4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata_CBS_138 Candida glabrata CBS 138]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CO4 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=1co4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1co4 OCA], [https://pdbe.org/1co4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1co4 RCSB], [https://www.ebi.ac.uk/pdbsum/1co4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1co4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMT1_CANGA AMT1_CANGA] Trans-acting regulatory protein that activates transcription of the MT genes (metallothionein) in response to copper or silver ions.
== 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/co/1co4_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=1co4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three dimensional structure of the N-terminal domain (residues 1-42) of the copper-responsive transcription factor Amtl from Candida glabrata has been determined by two-dimensional 1H-correlated nuclear magnetic resonance (NMR) methods. The domain contains an array of zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) that is conserved among a family of Cu-responsive transcription factors. The structure is unlike those of previously characterized zinc finger motifs, and consists of a three-stranded antiparallel beta-sheet with two short helical segments that project from one end of the beta-sheet. Conserved residues at positions 16, 18 and 19 form a basic patch that may be important for DNA binding.


==About this Structure==
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors.,Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:9665167<ref>PMID:9665167</ref>
1CO4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CO4 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors., Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR, Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9665167 9665167]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1co4" style="background-color:#fffaf0;"></div>
[[Category: Posewitz, M.C.]]
== References ==
[[Category: Smith, D.L.]]
<references/>
[[Category: Summers, M.F.]]
__TOC__
[[Category: Turner, R.B.]]
</StructureSection>
[[Category: Winge, D.R.]]
[[Category: Large Structures]]
[[Category: Zawrotny, M.E.]]
[[Category: Posewitz MC]]
[[Category: ZN]]
[[Category: Smith DL]]
[[Category: amt]]
[[Category: Summers MF]]
[[Category: metal regulation]]
[[Category: Turner RB]]
[[Category: metallothionein]]
[[Category: Winge DR]]
 
[[Category: Zawrotny ME]]
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