2qcp: Difference between revisions

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[[Image:2qcp.jpg|left|200px]]
{{Seed}}
[[Image:2qcp.png|left|200px]]


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{{STRUCTURE_2qcp|  PDB=2qcp  |  SCENE=  }}  
{{STRUCTURE_2qcp|  PDB=2qcp  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_17893365}}


==About this Structure==
==About this Structure==
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[[Category: Periplasmic]]
[[Category: Periplasmic]]
[[Category: Silver-binding]]
[[Category: Silver-binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 14:44:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:35:35 2008''

Revision as of 18:35, 28 July 2008

File:2qcp.png

Template:STRUCTURE 2qcp

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

Template:ABSTRACT PUBMED 17893365

About this Structure

2QCP is a Single protein structure of sequence from Escherichia coli. 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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