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1q06
From Proteopedia
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(New page: 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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Revision as of 22:09, 20 November 2007
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Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator
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.
About this Structure
1Q06 is a Single protein structure of sequence from Escherichia coli with AG as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 00:16:24 2007
