Publication Date:
2003-09-06
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changela, Anita -- Chen, Kui -- Xue, Yi -- Holschen, Jackie -- Outten, Caryn E -- O'Halloran, Thomas V -- Mondragon, Alfonso -- F32 DK61868/DK/NIDDK NIH HHS/ -- GM08382/GM/NIGMS NIH HHS/ -- GM38784/GM/NIGMS NIH HHS/ -- GM51350/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1383-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, 2205Tech Drive, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958362" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Bacterial Proteins/*chemistry/genetics/*metabolism
;
Binding Sites
;
Copper/*metabolism
;
Crystallization
;
Crystallography, X-Ray
;
DNA-Binding Proteins/*chemistry/genetics/*metabolism
;
Dimerization
;
Escherichia coli/*chemistry/genetics/metabolism
;
Escherichia coli Proteins/*chemistry/genetics/*metabolism
;
Helix-Turn-Helix Motifs
;
Hydrogen Bonding
;
Hydrophobic and Hydrophilic Interactions
;
Ligands
;
Metals/*metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Oxidation-Reduction
;
Promoter Regions, Genetic
;
Protein Conformation
;
Protein Structure, Secondary
;
Sequence Alignment
;
Thermodynamics
;
Transcription Factors/chemistry/genetics/metabolism
;
Transcriptional Activation
;
Zinc/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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