{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T07:01:13Z","timestamp":1790060473870,"version":"4.0.1"},"reference-count":41,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2019,1,30]],"date-time":"2019-01-30T00:00:00Z","timestamp":1548806400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2019,2]]},"abstract":"<jats:p>Frataxins form an interesting family of iron\u2010binding proteins with an almost unique fold and are highly conserved from bacteria to primates. They have a pivotal role in iron\u2013sulfur 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\u2010ray structure of frataxin from the thermophilic fungus <jats:italic>Chaetomium\u00a0thermophilum<\/jats:italic>, 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\u2010binding mode of Ct frataxin and demonstrated that it binds it through a semiconserved negatively charged ridge on the first helix and beta\u2010strand. Moreover, this frataxin is also able to bind the bacterial ortholog of the desulfurase, which is central in iron\u2013sulfur cluster synthesis, and act as its inhibitor.<\/jats:p>","DOI":"10.1111\/febs.14750","type":"journal-article","created":{"date-parts":[[2019,1,12]],"date-time":"2019-01-12T14:04:48Z","timestamp":1547301888000},"page":"495-506","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Structural and functional characterization of a frataxin from a thermophilic organism"],"prefix":"10.1111","volume":"286","author":[{"given":"Masooma","family":"Rasheed","sequence":"first","affiliation":[{"name":"King's College London UK"},{"name":"UK Dementia Research Institute at King's College London UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mostafa","family":"Jamshidiha","sequence":"additional","affiliation":[{"name":"Department of Life Sciences Imperial College London South Kensington 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