1q07: Difference between revisions

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==Crystal structure of the Au(I) form of E. coli CueR, a copper efflux regulator==
==Crystal structure of the Au(I) form of E. coli CueR, a copper efflux regulator==
<StructureSection load='1q07' size='340' side='right' caption='[[1q07]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1q07' size='340' side='right' caption='[[1q07]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q05|1q05]], [[1q06|1q06]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q05|1q05]], [[1q06|1q06]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CUER ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CUER ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q07 OCA], [http://pdbe.org/1q07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q07 RCSB], [http://www.ebi.ac.uk/pdbsum/1q07 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q07 OCA], [http://pdbe.org/1q07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q07 RCSB], [http://www.ebi.ac.uk/pdbsum/1q07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q07 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q0/1q07_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q0/1q07_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 11:29, 24 February 2018

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

Structural highlights

1q07 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:CUER ("Bacillus coli" Migula 1895)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Outten FW, Outten CE, Hale J, O'Halloran TV. Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, cueR. J Biol Chem. 2000 Oct 6;275(40):31024-9. PMID:10915804 doi:http://dx.doi.org/10.1074/jbc.M006508200
  2. ↑ Outten FW, Huffman DL, Hale JA, O'Halloran TV. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem. 2001 Aug 17;276(33):30670-7. Epub 2001 Jun 8. PMID:11399769 doi:http://dx.doi.org/10.1074/jbc.M104122200
  3. ↑ Changela A, Chen K, Xue Y, Holschen J, Outten CE, O'Halloran TV, Mondragon A. Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR. Science. 2003 Sep 5;301(5638):1383-7. PMID:12958362 doi:http://dx.doi.org/10.1126/science.1085950

1q07, resolution 2.50Å

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