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Biomol NMR Assign. 2019 Oct;13(2):377-381. doi: 10.1007/s12104-019-09910-0. Epub 2019 Aug 22.

Backbone resonance assignments and secondary structure of the apo-Drosophila melanogaster frataxin homolog (Dfh).

Author information

1
Department of Biochemistry and Molecular Biology, Wayne State University, Detroit, MI, 48201, USA.
2
Department of Natural Sciences, University of Michigan - Dearborn, Dearborn, MI, 48128, USA.
3
Department of Biochemistry and Molecular Biology, Wayne State University, Detroit, MI, 48201, USA. tstemmle@med.wayne.edu.
4
Department of Pharmaceutical Sciences, Wayne State University, Detroit, MI, 48201, USA. tstemmle@med.wayne.edu.

Abstract

Friedreich's ataxia, the most prevalent hereditary ataxia, is caused by a patient's inability to produce a viable form of the protein frataxin. Frataxin plays an essential role in cellular iron regulation and has been shown to participate in the assembly of iron-sulfur (Fe-S) clusters under a variety of roles, including modulating persulfide production and directing Fe(II) delivery to the assembly scaffold protein. While the activity and structure of multiple eukaryotic frataxin orthologs have been characterized, the fly ortholog has numerous advantages over other orthologs with regards to protein stability, its activity towards Fe-S cluster assembly and its stability for forming stable proteins partner assemblies. Given the obvious advantages for studying the Drosophila melanogaster frataxin homolog (Dfh) over its orthologs, we have undertaken a structural characterization of apo-Dfh as the first step towards solving the solution structure of the protein alone and in complex with protein partners within the Fe-S cluster assembly pathway.

KEYWORDS:

Fe–S scaffold protein; Frataxin; Friedreich’s ataxia; Iron sulfur cluster; IscU; Isu1; NMR assignments

PMID:
31440902
DOI:
10.1007/s12104-019-09910-0

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