6fco

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

spinqualitylabelsall models 6fco, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fco is a 6 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.03Å Ligands: MLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0S1Z8_CHATD Publication Abstract from PubMed 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. Structural and functional characterization of a frataxin from a thermophilic organism.,Rasheed M, Jamshidiha M, Puglisi R, Yan R, Cota E, Pastore A FEBS J. 2019 Feb;286(3):495-506. doi: 10.1111/febs.14750. Epub 2019 Jan 30. PMID:30636112 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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