Ontology highlight
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 t
SUBMITTER: Kulathila R
PROVIDER: S-EPMC3017539 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature