Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump

While copper has essential functions as an enzymatic co-factor, excess copper ions are toxic for cells, necessitating mechanisms for regulating its levels. The cusCBFA operon of E. coli encodes a four-component efflux pump dedicated to the extrusion of Cu(I) and Ag(I) ions. We have solved the X-ray...

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Bibliographic Details
Published in:PloS one 2011-01, Vol.6 (1), p.e15610
Main Authors: Kulathila, Rithika, Kulathila, Ragini, Indic, Mridhu, van den Berg, Bert
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
BASIC BIOLOGICAL SCIENCES
Binding sites
Biology
Cadmium
Chromosomes
Cloning
Collaboration
COPPER
Copper - chemistry
Copper - metabolism
COPPER IONS
CRYSTAL STRUCTURE
Crystallography
Crystallography, X-Ray
E coli
Efflux
Enzymes
ESCHERICHIA COLI
Escherichia coli - chemistry
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Exports
EXTRUSION
FUNCTIONS
HEAVY METALS
Inner membranes
Ionizing radiation
IONS
Kinases
LEVELS
LIPIDS
Medical schools
Medicine
Membrane proteins
Membrane Proteins - chemistry
Membrane Proteins - metabolism
MEMBRANES
METALS
Metals, Heavy - metabolism
Models, Molecular
Operons
Outer membranes
Protein Structure, Quaternary
Protein Structure, Tertiary
PROTEINS
Pseudomonas aeruginosa
RESOLUTION
Silver
Silver - chemistry
Silver - metabolism
SPECIFICITY
Substrate Specificity
SUBSTRATES
TOXICITY
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Summary:While copper has essential functions as an enzymatic co-factor, excess copper ions are toxic for cells, necessitating mechanisms for regulating its levels. The cusCBFA operon of E. coli encodes a four-component efflux pump dedicated to the extrusion of Cu(I) and Ag(I) ions. We have solved the X-ray crystal structure of CusC, the outer membrane component of the Cus heavy metal efflux pump, to 2.3 Å resolution. The structure has the largest extracellular opening of any outer membrane factor (OMF) protein and suggests, for the first time, the presence of a tri-acylated N-terminal lipid anchor. The CusC protein does not have any obvious features that would make it specific for metal ions, suggesting that the narrow substrate specificity of the pump is provided by other components of the pump, most likely by the inner membrane component CusA.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0015610