Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters

Yoshimitsu Kakuta, T. Horio, Y. Takahashi, K. Fukuyama

Research output: Contribution to journalArticle

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Abstract

Escherichia coli ferredoxin (Fdx) is an adrenodoxin-type [2Fe-2S] ferredoxin. Recent genetic analyses show that it has an esssential 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 Rfree values of 0.255 and 0.278, respectively, at 1.7 Å 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 Cα atoms are 1.8 and 2.2 Å. 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 Sγ 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.

Original languageEnglish
Pages (from-to)11007-11012
Number of pages6
JournalBiochemistry
Volume40
Issue number37
DOIs
Publication statusPublished - Sep 18 2001
Externally publishedYes

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Adrenodoxin
Ferredoxins
Sulfur
Escherichia coli
Iron
Crystal structure
Atoms
Ferredoxin-NADP Reductase
Pseudomonas putida
Protein S
Static Electricity
Machinery
Electrostatics
Wavelength
Molecules
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters. / Kakuta, Yoshimitsu; Horio, T.; Takahashi, Y.; Fukuyama, K.

In: Biochemistry, Vol. 40, No. 37, 18.09.2001, p. 11007-11012.

Research output: Contribution to journalArticle

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abstract = "Escherichia coli ferredoxin (Fdx) is an adrenodoxin-type [2Fe-2S] ferredoxin. Recent genetic analyses show that it has an esssential 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 Rfree values of 0.255 and 0.278, respectively, at 1.7 {\AA} 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 Cα atoms are 1.8 and 2.2 {\AA}. 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 Sγ 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.",
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