1q07
Crystal structure of the Au(I) form of E. coli CueR, a copper efflux regulatorCrystal structure of the Au(I) form of E. coli CueR, a copper efflux regulator
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||