A novel copper-binding fold for the periplasmic copper resistance protein CusF

Isabell R. Loftin, Sylvia Franke, Sue A. Roberts, Andrzej Weichsel, Annie Héroux, William R. Montfort, Christopher Rensing, Megan M. McEvoy

Research output: Contribution to journalArticlepeer-review

102 Scopus citations


We have determined the crystal structure of apo-CusF, a periplasmic protein involved in copper and silver resistance in Escherichia coli. The protein forms a five-stranded β-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in β-strands 2 and 3. These residues are clustered at one end of the β-barrel, and their side chains are oriented toward the interior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structural changes using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF are distinct from those of previously characterized copper-binding proteins.

Original languageEnglish (US)
Pages (from-to)10533-10540
Number of pages8
Issue number31
StatePublished - Aug 9 2005

ASJC Scopus subject areas

  • Biochemistry


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