1Q07

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

Summary for 1Q07

• Entry DOI: 10.2210/pdb1q07/pdb
• Related: 1Q05 1Q06
• Descriptor: Transcriptional regulator cueR, GOLD ION (3 entities in total)
• Functional Keywords: merr family transcriptional regulator, copper efflux regulator, transcription
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Probable): P0A9G4
• Total number of polymer chains: 2
• Total formula weight: 30906.27

Authors

Changela, A.,Chen, K.,Xue, Y.,Holschen, J.,Outten, C.E.,O'Halloran, T.V.,Mondragon, A. (deposition date: 2003-07-15, release date: 2003-09-16, Last modification date: 2024-02-14)

Primary citation

Changela, A.,Chen, K.,Xue, Y.,Holschen, J.,Outten, C.E.,O'Halloran, T.V.,Mondragon, A.
Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR
Science, 301:1383-1387, 2003

PubMed Abstract: 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.

PubMed: 12958362
DOI: 10.1126/science.1085950

Experimental method

X-RAY DIFFRACTION (2.5 Å)