1q06: Difference between revisions

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New page: left|200px<br /><applet load="1q06" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q06, resolution 2.07Å" /> '''Crystal structure of...
 
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[[Image:1q06.gif|left|200px]]<br /><applet load="1q06" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q06, resolution 2.07&Aring;" />
'''Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator'''<br />


==Overview==
==Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator==
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.
<StructureSection load='1q06' size='340' side='right'caption='[[1q06]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1q06]] 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=1Q06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q06 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.07&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG:SILVER+ION'>AG</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=1q06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q06 OCA], [https://pdbe.org/1q06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q06 RCSB], [https://www.ebi.ac.uk/pdbsum/1q06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q06 ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/q0/1q06_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=1q06 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1Q06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with AG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q06 OCA].
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12958362 12958362]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Changela, A.]]
[[Category: Changela A]]
[[Category: Chen, K.]]
[[Category: Chen K]]
[[Category: Halloran, T.V.O.]]
[[Category: Holschen J]]
[[Category: Holschen, J.]]
[[Category: Mondragon A]]
[[Category: Mondragon, A.]]
[[Category: O'Halloran TV]]
[[Category: Outten, C.E.]]
[[Category: Outten CE]]
[[Category: Xue, Y.]]
[[Category: Xue Y]]
[[Category: AG]]
[[Category: copper efflux regulator]]
[[Category: merr family transcriptional regulator]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:16:24 2007''

Latest revision as of 11:11, 14 February 2024

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

Structural highlights

1q06 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.07Å
Ligands:
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.

See Also

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

1q06, resolution 2.07Å

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