2QCP

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

Summary for 2QCP

• Entry DOI: 10.2210/pdb2qcp/pdb
• Related: 1zeq
• Descriptor: Cation efflux system protein cusF, NITRATE ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: silver-binding, copper-binding, beta barrel, ob-fold, metalloprotein, metal resistance, metal-binding, periplasmic, metal binding protein
• Biological source: Escherichia coli str. K12 substr.
• Cellular location: Periplasm: P77214
• Total number of polymer chains: 1
• Total formula weight: 9315.28

Authors

Loftin, I.R. (deposition date: 2007-06-19, release date: 2007-10-02, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1 Å)