A Novel Copper-Binding Fold for the Periplasmic Copper Resistance Protein CusF
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- 作者：Isabell R. Loftin ; Sylvia Franke ; Sue A. Roberts ; Andrzej Weichsel ; Annie Hé ; roux ; William R. Montfort ; Christopher Rensing ; and Megan M. McEvoy
- 刊名：Biochemistry
- 出版年：2005
- 出版时间：August 9, 2005
- 年：2005
- 卷：44
- 期：31
- 页码：10533 - 10540
- 全文大小：722K
- 年卷期：v.44,no.31(August 9, 2005)
- ISSN：1520-4995
文摘
We have determined the crystal structure of apo-CusF, a periplasmic protein involved in copperand silver resistance in Escherichia coli. The protein forms a five-stranded 
-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experimentssuggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in -strands 2 and 3.These residues are clustered at one end of the -barrel, and their side chains are oriented toward theinterior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structuralchanges using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF aredistinct from those of previously characterized copper-binding proteins.
-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experimentssuggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in -strands 2 and 3.These residues are clustered at one end of the -barrel, and their side chains are oriented toward theinterior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structuralchanges using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF aredistinct from those of previously characterized copper-binding proteins.