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''' | ||
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[[Category: Outten, C E.]] | [[Category: Outten, C E.]] | ||
[[Category: Xue, Y.]] | [[Category: Xue, Y.]] | ||
[[Category: | [[Category: Copper efflux regulator]] | ||
[[Category: | [[Category: Merr family transcriptional regulator]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:42:27 2008'' | |||
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Revision as of 05:42, 3 May 2008
Crystal structure of the Au(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
1Q07 is a Single protein structure of sequence from Escherichia coli. 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 Page seeded by OCA on Sat May 3 05:42:27 2008