Backbone Resonance Assignments and Secondary Structure of the Apo-Drosophila Melanogaster Frataxin Homolog (Dfh)

Overview

Journal Biomol NMR Assign

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2019 Aug 24

PMID 31440902

Citations 1

Authors

Swati Rawat

Kalyan C Kondapalli

Andria V Rodrigues

Timothy L Stemmler

Affiliations

Soon will be listed here.

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.

Citing Articles

Drosophila melanogaster frataxin: protein crystal and predicted solution structure with identification of the iron-binding regions.

Rodrigues A, Batelu S, Hinton T, Rotondo J, Thompson L, Brunzelle J Acta Crystallogr D Struct Biol. 2023; 79(Pt 1):22-30.

PMID: 36601804 PMC: 9815096. DOI: 10.1107/S2059798322011639.

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