Please use this identifier to cite or link to this item:
Title: Frataxin Structure and Function
Authors: Castro, Ignacio Hugo 
Pignataro, María Florencia 
Sewell, Karl Ellioth 
Espeche, Lucía Daniela 
Herrera, María Georgina 
Noguera, Martín Ezequiel 
Dain, Liliana 
Nadra, Alejandro Daniel 
Aran, Martín 
Smal, Clara 
Gallo, Mariana 
Santos, Javier 
Keywords: Tipificación Molecular;Proteínas Mitocondriales
Issue Date: 2019
Journal: Sub-cellular biochemistry 
Abstract: Mammalian frataxin is a small mitochondrial protein involved in iron sulfur cluster assembly. Frataxin deficiency causes the neurodegenerative disease Friedreich's Ataxia. Valuable knowledge has been gained on the structural dynamics of frataxin, metal-ion-protein interactions, as well as on the effect of mutations on protein conformation, stability and internal motions. Additionally, laborious studies concerning the enzymatic reactions involved have allowed for understanding the capability of frataxin to modulate Fe-S cluster assembly function. Remarkably, frataxin biological function depends on its interaction with some proteins to form a supercomplex, among them NFS1 desulfurase and ISCU, the scaffolding protein. By combining multiple experimental tools including high resolution techniques like NMR and X-ray, but also SAXS, crosslinking and mass-spectrometry, it was possible to build a reliable model of the structure of the desulfurase supercomplex NFS1/ACP-ISD11/ISCU/frataxin. In this chapter, we explore these issues showing how the scientific view concerning frataxin structure-function relationships has evolved over the last years.
Description: Fil: Dain, Liliana. ANLIS Dr.C.G.Malbrán. Centro Nacional de Genética Médica Dr. Eduardo Castilla; Argentina.
ISSN: 0306-0225
DOI: 10.1007/978-3-030-28151-9_13
Appears in Collections:Publicaciones CeNaGeM

Show full item record

Page view(s)

checked on Jun 6, 2020

Google ScholarTM




Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.