1ZEQ : 1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli

  • Christopher Rensing (Contributor)
  • Megan M. McEvoy (Contributor)
  • Isabell R. Loftin (Contributor)
  • Sylvia Franke (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.5
Classification:METAL BINDING PROTEIN
Release Date:2005-08-02
Deposition Date:2005-04-19
Revision Date:2008-04-30#2011-07-13
Molecular Weight:9339.76
Macromolecule Type:Protein
Residue Count:84
Atom Site Count:669
DOI:10.2210/pdb1zeq/pdb

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.
Date made available2005
PublisherRCSB-PDB

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