The biosynthesis of Fe-S clusters is a vital process involving the delivery of iron and sulfur to scaffold proteins via molecular interactions that are still poorly defined. They reconstituted a stable, functional complex consisting of the iron donor, Yfh1, and the Fe-S cluster scaffold, Isu1, with 1:1 stoichiometry. They used this to develop a three-dimensional reconstruction of this complex. Through further work, they also identified protein-protein interaction surfaces within the complex. The data suggests that the proposed structure is suitable to ensure concerted and protected transfer of potentially toxic iron and sulfur atoms to Isu1 during Fe-S cluster assembly. Frataxin is involved in this process, so developing an understanding of how this structure functions allows us to interpret frataxin's precise role, and the roles of parts of the molecule where FA-causing mutations occur.
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