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

ABSTRACT:

Background

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.

Methodology/principal findings

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.

Conclusions/significance

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.

SUBMITTER: Kulathila R

PROVIDER: S-EPMC3017539 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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

Kulathila Rithika R Kulathila Ragini R Indic Mridhu M van den Berg Bert B

PloS one 20110107 1

<h4>Background</h4>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.<h4>Methodology/principal findings</h4>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 ...[more]

PMID: 21249122

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