1q09

<table><tr><td colspan='2'>[[1q09]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q09 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q09 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q08|1q08]], [[1q0a|1q0a]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZNTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q09 OCA], [http://pdbe.org/1q09 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q09 RCSB], [http://www.ebi.ac.uk/pdbsum/1q09 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q09 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ZNTR_ECOLI ZNTR_ECOLI]] Zinc-responsive transcriptional regulator of zntA.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The earliest of a series of copper efflux genes in Escherichia coli are controlled by CueR, a member of the MerR family of transcriptional activators. Thermodynamic calibration of CueR reveals a zeptomolar (10(-21) molar) sensitivity to free Cu+, which is far less than one atom per cell. Atomic details of this extraordinary sensitivity and selectivity for +1transition-metal ions are revealed by comparing the crystal structures of CueR and a Zn2+-sensing homolog, ZntR. An unusual buried metal-receptor site in CueR restricts the metal to a linear, two-coordinate geometry and uses helix-dipole and hydrogen-bonding interactions to enhance metal binding. This binding mode is rare among metalloproteins but well suited for an ultrasensitive genetic switch.

Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR.,Changela A, Chen K, Xue Y, Holschen J, Outten CE, O'Halloran TV, Mondragon A Science. 2003 Sep 5;301(5638):1383-7. PMID:12958362<ref>PMID:12958362</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1q09" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Changela, A]]

[[Category: Chen, K]]

[[Category: Halloran, T V.O]]

[[Category: Holschen, J]]

[[Category: Mondragon, A]]

[[Category: Outten, C E]]

[[Category: Xue, Y]]

[[Category: Merr family transcriptional regulator]]

[[Category: Transcription]]