2qcp
From Proteopedia
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1.0 A Structure of CusF-Ag(I) residues 10-88 from Escherichia coli
Overview
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.
About this Structure
2QCP is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.
Reference
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy., Loftin IR, Franke S, Blackburn NJ, McEvoy MM, Protein Sci. 2007 Oct;16(10):2287-93. PMID:17893365
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