1zeq

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|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])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zeq OCA], [http://www.ebi.ac.uk/pdbsum/1zeq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zeq RCSB]</span>
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[[Category: ob-fold]]
[[Category: ob-fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:54 2008''

Revision as of 22:34, 30 March 2008


PDB ID 1zeq

Drag the structure with the mouse to rotate
, resolution 1.50Å
Gene: cusF, cusX (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli


Overview

We have determined the crystal structure of apo-CusF, a periplasmic protein involved in copper and silver resistance in Escherichia coli. The protein forms a five-stranded beta-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered at one end of the beta-barrel, and their side chains are oriented toward the interior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structural changes using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF are distinct from those of previously characterized copper-binding proteins.

About this Structure

1ZEQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A novel copper-binding fold for the periplasmic copper resistance protein CusF., Loftin IR, Franke S, Roberts SA, Weichsel A, Heroux A, Montfort WR, Rensing C, McEvoy MM, Biochemistry. 2005 Aug 9;44(31):10533-40. PMID:16060662

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