1q06: Difference between revisions
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=" | [[Image:1q06.gif|left|200px]]<br /><applet load="1q06" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1q06, resolution 2.07Å" /> | caption="1q06, resolution 2.07Å" /> | ||
'''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 | 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:// | 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== | ||
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[[Category: Changela, A.]] | [[Category: Changela, A.]] | ||
[[Category: Chen, K.]] | [[Category: Chen, K.]] | ||
[[Category: Halloran, T | [[Category: Halloran, T V.O.]] | ||
[[Category: Holschen, J.]] | [[Category: Holschen, J.]] | ||
[[Category: Mondragon, A.]] | [[Category: Mondragon, A.]] | ||
[[Category: Outten, C | [[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:// | ''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
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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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