2qcp
From Proteopedia
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|PDB= 2qcp |SIZE=350|CAPTION= <scene name='initialview01'>2qcp</scene>, resolution 1.000Å | |PDB= 2qcp |SIZE=350|CAPTION= <scene name='initialview01'>2qcp</scene>, resolution 1.000Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AG:SILVER+ION'>AG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= cusF, cusX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= cusF, cusX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1zeq|1zeq]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcp OCA], [http://www.ebi.ac.uk/pdbsum/2qcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qcp RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Loftin, I R.]] | [[Category: Loftin, I R.]] | ||
- | [[Category: AG]] | ||
- | [[Category: NO3]] | ||
- | [[Category: SO4]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: copper-binding]] | [[Category: copper-binding]] | ||
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[[Category: silver-binding]] | [[Category: silver-binding]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:47:51 2008'' |
Revision as of 01:47, 31 March 2008
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, resolution 1.000Å | |||||||
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Ligands: | , , | ||||||
Gene: | cusF, cusX (Escherichia coli) | ||||||
Related: | 1zeq
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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