1i7h

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Revision as of 18:00, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1i7h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i7h, resolution 1.70Å" /> '''CRYSTAL STURCUTURE O...)
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File:1i7h.gif


1i7h, resolution 1.70Å

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CRYSTAL STURCUTURE OF FDX

OverviewOverview

Escherichia coli ferredoxin (Fdx) is an adrenodoxin-type [2Fe-2S], ferredoxin. Recent genetic analyses show that it has an essential role in, the maturation of various iron-sulfur (Fe-S) proteins. Fdx probably, functions as a component of the complex machinery responsible for the, biogenesis of Fe-S clusters. Its crystal structure was determined by the, multiple-wavelength anomalous dispersion method using the iron atoms in, the [2Fe-2S] cluster of the protein and then refined to R and R(free), values of 0.255 and 0.278, respectively, at 1.7 A resolution. The, structure of Fdx is similar to the structures of bovine adrenodoxin (Adx), and Pseudomonas putida putidaredoxin (Pdx) whose respective, root-mean-square deviations of the corresponding Calpha atoms are 1.8 and, 2.2 A. This analysis also revealed the structure of the C-terminal, residues protruding into the solvent, which is missing in Adx and Pdx. The, [2Fe-2S] cluster is located at the edge of the molecule and bonds with the, Sgamma atoms of Cys42, Cys48, Cys51, and Cys87. Electrostatic potential, analysis showed that the surface of Fdx has two negatively charged areas, separated by a hydrophobic lane. One is conserved on the surface of Adx, which is an area of interaction with adrenodoxin reductase. Cys46 is, located on the molecular surface in the vicinity of the [2Fe-2S] cluster, an indication that it may be involved in Fe-S cluster formation.

About this StructureAbout this Structure

1I7H is a Single protein structure of sequence from Escherichia coli with FES as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters., Kakuta Y, Horio T, Takahashi Y, Fukuyama K, Biochemistry. 2001 Sep 18;40(37):11007-12. PMID:11551196

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