1zeq
From Proteopedia
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1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli
Overview
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.
About this Structure
1ZEQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A novel copper-binding fold for the periplasmic copper resistance protein CusF., Loftin IR, Franke S, Roberts SA, Weichsel A, Heroux A, Montfort WR, Rensing C, McEvoy MM, Biochemistry. 2005 Aug 9;44(31):10533-40. PMID:16060662
Page seeded by OCA on Wed Nov 21 07:25:04 2007
