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"  
[[Image:1q06.gif|left|200px]]<br /><applet load="1q06" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1q06, resolution 2.07&Aring;" />
caption="1q06, resolution 2.07&Aring;" />
'''Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator'''<br />
'''Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
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].  
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 <scene name='pdbligand=AG:'>AG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q06 OCA].  


==Reference==
==Reference==
Line 15: Line 15:
[[Category: Changela, A.]]
[[Category: Changela, A.]]
[[Category: Chen, K.]]
[[Category: Chen, K.]]
[[Category: Halloran, T.V.O.]]
[[Category: Halloran, T V.O.]]
[[Category: Holschen, J.]]
[[Category: Holschen, J.]]
[[Category: Mondragon, A.]]
[[Category: Mondragon, A.]]
[[Category: Outten, C.E.]]
[[Category: Outten, C E.]]
[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
[[Category: AG]]
[[Category: AG]]
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[[Category: merr family transcriptional regulator]]
[[Category: merr family transcriptional regulator]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:16:24 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:31 2008''

Revision as of 15:34, 21 February 2008

File:1q06.gif


1q06, resolution 2.07Å

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

OverviewOverview

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.

About this StructureAbout this Structure

1Q06 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

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