2QCP

1.0 A Structure of CusF-Ag(I) residues 10-88 from Escherichia coli

2QCP の概要

• エントリーDOI: 10.2210/pdb2qcp/pdb
• 関連するPDBエントリー: 1zeq
• 分子名称: Cation efflux system protein cusF, NITRATE ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: silver-binding, copper-binding, beta barrel, ob-fold, metalloprotein, metal resistance, metal-binding, periplasmic, metal binding protein
• 由来する生物種: Escherichia coli str. K12 substr.
• 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: 9315.28

構造登録者

Loftin, I.R. (登録日: 2007-06-19, 公開日: 2007-10-02, 最終更新日: 2023-08-30)

主引用文献

Loftin, I.R.,Franke, S.,Blackburn, N.J.,McEvoy, M.M.
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy
Protein Sci., 16:2287-2293, 2007

PubMed Abstract: Elevated levels of copper or silver ions in the environment are an immediate threat to many organisms. Escherichia coli is able to resist the toxic effects of these ions through strictly limiting intracellular levels of Cu(I) and Ag(I). The CusCFBA system is one system in E. coli responsible for copper/silver tolerance. A key component of this system is the periplasmic copper/silver-binding protein, CusF. Here the X-ray structure and XAS data on the CusF-Ag(I) and CusF-Cu(I) complexes, respectively, are reported. In the CusF-Ag(I) structure, Ag(I) is coordinated by two methionines and a histidine, with a nearby tryptophan capping the metal site. EXAFS measurements on the CusF-Cu(I) complex show a similar environment for Cu(I). The arrangement of ligands effectively sequesters the metal from its periplasmic environment and thus may play a role in protecting the cell from the toxic ion.

PubMed: 17893365
DOI: 10.1110/ps.073021307

実験手法

X-RAY DIFFRACTION (1 Å)