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1q05

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[[Image:1q05.gif|left|200px]]
 
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==Crystal structure of the Cu(I) form of E. coli CueR, a copper efflux regulator==
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The line below this paragraph, containing "STRUCTURE_1q05", creates the "Structure Box" on the page.
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<StructureSection load='1q05' size='340' side='right'caption='[[1q05]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1q05]] 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=1Q05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q05 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#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=CU1:COPPER+(I)+ION'>CU1</scene></td></tr>
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{{STRUCTURE_1q05| PDB=1q05 | SCENE= }}
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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=1q05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q05 OCA], [https://pdbe.org/1q05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q05 RCSB], [https://www.ebi.ac.uk/pdbsum/1q05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q05 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CUER_ECOLI CUER_ECOLI] Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.<ref>PMID:10915804</ref> <ref>PMID:11399769</ref>
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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/q0/1q05_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1q05 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the Cu(I) form of E. coli CueR, a copper efflux regulator'''
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==See Also==
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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1Q05 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q05 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12958362 12958362]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Changela, A.]]
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[[Category: Changela A]]
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[[Category: Chen, K.]]
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[[Category: Chen K]]
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[[Category: Halloran, T V.O.]]
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[[Category: Holschen J]]
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[[Category: Holschen, J.]]
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[[Category: Mondragon A]]
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[[Category: Mondragon, A.]]
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[[Category: O'Halloran TV]]
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[[Category: Outten, C E.]]
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[[Category: Outten CE]]
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[[Category: Xue, Y.]]
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[[Category: Xue Y]]
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[[Category: Copper efflux regulator]]
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[[Category: Merr family transcriptional regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:42:18 2008''
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Current revision

Crystal structure of the Cu(I) form of E. coli CueR, a copper efflux regulator

PDB ID 1q05

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