1ZEQ

1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli

Summary for 1ZEQ

• Entry DOI: 10.2210/pdb1zeq/pdb
• Descriptor: Cation efflux system protein cusF (2 entities in total)
• Functional Keywords: copper-binding, ob-fold, beta barrel, metallochaperone, metal binding protein
• Biological source: Escherichia coli
• Cellular location: Periplasm: P77214
• Total number of polymer chains: 1
• Total formula weight: 9339.76

Authors

Loftin, I.R.,Franke, S.,Roberts, S.A.,Weichsel, A.,Heroux, A.,Montfort, W.R.,Rensing, C.,McEvoy, M.M. (deposition date: 2005-04-19, release date: 2005-08-02, Last modification date: 2024-02-14)

Primary citation

Loftin, I.R.,Franke, S.,Roberts, S.A.,Weichsel, A.,Montfort, W.R.,Rensing, C.,McEvoy, M.M.
A Novel Copper-Binding Fold for the Periplasmic Copper Resistance Protein CusF.
Biochemistry, 44:10533-10540, 2005

PubMed Abstract: 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 beta-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 beta-strands 2 and 3. These residues are clustered at one end of the beta-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.

PubMed: 16060662
DOI: 10.1021/bi050827b

Experimental method

X-RAY DIFFRACTION (1.5 Å)