1ZEQ

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

1ZEQ の概要

• エントリーDOI: 10.2210/pdb1zeq/pdb
• 分子名称: Cation efflux system protein cusF (2 entities in total)
• 機能のキーワード: copper-binding, ob-fold, beta barrel, metallochaperone, metal binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P77214
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9339.76

構造登録者

Loftin, I.R.,Franke, S.,Roberts, S.A.,Weichsel, A.,Heroux, A.,Montfort, W.R.,Rensing, C.,McEvoy, M.M. (登録日: 2005-04-19, 公開日: 2005-08-02, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.5 Å)