Asp97 is a crucial residue involved in the ligation of the [Fe₄S₄] cluster of IscA from Acidithiobacillus ferrooxidans
IscA was proposed to be involved in the iron-sulfur cluster assembly encoded by the iscSUA operon, but the role of IscA in the iron-sulfur cluster assembly still remains controversial. In our previous study, the IscA from A. ferrooxidans was successfully expressed in Escherichia coli, and purified t...
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Veröffentlicht in: | Journal of microbiology and biotechnology 2008-06, Vol.18 (6), p.1070-1075 |
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Zusammenfassung: | IscA was proposed to be involved in the iron-sulfur cluster assembly encoded by the iscSUA operon, but the role of IscA in the iron-sulfur cluster assembly still remains controversial. In our previous study, the IscA from A. ferrooxidans was successfully expressed in Escherichia coli, and purified to be a [Fe₄S₄]-cluster-containing protein. Cys35, Cys99, and Cys101 were important residues in ligating with the [Fe₄S₄] cluster. In this study, Asp97 was found to be another ligand for the iron-sulfur cluster binding according to site-directed mutagenesis results. Molecular modeling for the IscA also showed that Asp97 was a strong ligand with the [Fe₄S₄] cluster, which was in good agreement with the experimental results. Thus, the [Fe₄S₄] cluster in IscA from A. ferrooxidans was ligated by three cysteine residues and one aspartic acid. |
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ISSN: | 1017-7825 |