Structural characterization of metal binding to a cold-adapted frataxin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-06

AUTHORS

Martín E. Noguera, Ernesto A. Roman, Juan B. Rigal, Alexandra Cousido-Siah, André Mitschler, Alberto Podjarny, Javier Santos

ABSTRACT

Frataxin is an evolutionary conserved protein that participates in iron metabolism. Deficiency of this small protein in humans causes a severe neurodegenerative disease known as Friedreich's ataxia. A number of studies indicate that frataxin binds iron and regulates Fe-S cluster biosynthesis. Previous structural studies showed that metal binding occurs mainly in a region of high density of negative charge. However, a comprehensive characterization of the binding sites is required to gain further insights into the mechanistic details of frataxin function. In this work, we have solved the X-ray crystal structures of a cold-adapted frataxin from a psychrophilic bacterium in the presence of cobalt or europium ions. We have identified a number of metal-binding sites, mainly solvent exposed, several of which had not been observed in previous studies on mesophilic homologues. No major structural changes were detected upon metal binding, although the structures exhibit significant changes in crystallographic B-factors. The analysis of these B-factors, in combination with crystal packing and RMSD among structures, suggests the existence of localized changes in the internal motions. Based on these results, we propose that bacterial frataxins possess binding sites of moderate affinity for a quick capture and transfer of iron to other proteins and for the regulation of Fe-S cluster biosynthesis, modulating interactions with partner proteins. More... »

PAGES

653-664

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00775-015-1251-9

DOI

http://dx.doi.org/10.1007/s00775-015-1251-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1023914887

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25832196


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