Imperial College London
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Dr Ernesto Cota

Faculty of Natural Sciences, Department of Life Sciences

Senior Lecturer
 
 
 
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Contact

 

+44 (0)20 7594 3689e.cota Website

 
 
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Location

 

601Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Rasheed:2019:10.1111/febs.14750,
author = {Rasheed, M and Jamshidiha, M and Puglisi, R and Yan, R and Cota, E and Pastore, A},
doi = {10.1111/febs.14750},
journal = {FEBS Journal},
pages = {495--506},
title = {Structural and functional characterization of a frataxin from a thermophilic organism},
url = {http://dx.doi.org/10.1111/febs.14750},
volume = {286},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Frataxins form an interesting family of ironbinding proteins with an almost unique fold and are highly conserved from bacteria to primates. They have a pivotal role in iron–sulfur cluster biogenesis as regulators of the rates of cluster formation, as it is testified by the fact that frataxin absence is incompatible with life and reduced levels of the protein lead to the recessive neurodegenerative disease Friedreich's ataxia. Despite its importance, the structure of frataxin has been solved only from relatively few species. Here, we discuss the Xray structure of frataxin from the thermophilic fungus Chaetomium thermophilum, and the characterization of its interactions and dynamics in solution. We show that this eukaryotic frataxin has an unusual variation in the classical frataxin fold: the last helix is shorter than in other frataxins which results in a less symmetrical and compact structure. The stability of this protein is comparable to that of human frataxin, currently the most stable among the frataxin orthologues. We also characterized the ironbinding mode of Ct frataxin and demonstrated that it binds it through a semiconserved negatively charged ridge on the first helix and betastrand. Moreover, this frataxin is also able to bind the bacterial ortholog of the desulfurase, which is central in iron–sulfur cluster synthesis, and act as its inhibitor.
AU  - Rasheed,M
AU  - Jamshidiha,M
AU  - Puglisi,R
AU  - Yan,R
AU  - Cota,E
AU  - Pastore,A
DO  - 10.1111/febs.14750
EP  - 506
PY  - 2019///
SN  - 0014-2956
SP  - 495
TI  - Structural and functional characterization of a frataxin from a thermophilic organism
T2  - FEBS Journal
UR  - http://dx.doi.org/10.1111/febs.14750
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000457745200006&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/69633
VL  - 286
ER  -
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