Asp97 is a Crucial Residue Involved in the Ligation of the [$Fe_4S_4$] Cluster of IscA from Acidithiobacillus ferrooxidans

  • Jiang, Huidan (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Zhang, Xiaojian (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Ai, Chenbing (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Liu, Yuandong (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Liu, Jianshe (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Qiu, Guanahou (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Zeng, Jia (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University)
  • Published : 2008.06.30

Abstract

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 [$Fe_4S_4$] -cluster-containing protein. Cys35, Cys99, and Cys101 were important residues in ligating with the [$Fe_4S_4$] 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 [$Fe_4S_4$] cluster, which was in good agreement with the experimental results. Thus, the [$Fe_4S_4$] cluster in IscA from A. ferrooxidans was ligated by three cysteine residues and one aspartic acid.

Keywords

References

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