6FCO

Structural and functional characterisation of Frataxin (FXN) like protein from Chaetomium thermophilum

6FCO の概要

• エントリーDOI: 10.2210/pdb6fco/pdb
• 分子名称: Mitochondrial frataxin-like protein, MALONIC ACID (3 entities in total)
• 機能のキーワード: iron sulphur cluster, iron chaperone, friedreich's ataxia, transport protein
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 85788.07

構造登録者

Jamshidiha, M.,Rasheed, M.,Pastore, A.,Cota, E. (登録日: 2017-12-20, 公開日: 2019-01-23, 最終更新日: 2024-05-08)

主引用文献

Rasheed, M.,Jamshidiha, M.,Puglisi, R.,Yan, R.,Cota, E.,Pastore, A.
Structural and functional characterization of a frataxin from a thermophilic organism.
FEBS J., 286:495-506, 2019

PubMed Abstract: Frataxins form an interesting family of iron-binding 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 X-ray 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 iron-binding mode of Ct frataxin and demonstrated that it binds it through a semiconserved negatively charged ridge on the first helix and beta-strand. 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.

PubMed: 30636112
DOI: 10.1111/febs.14750

実験手法

X-RAY DIFFRACTION (2.03 Å)