Abstract:
:Iron-sulfur (Fe-S) proteins are key players in vital processes involving energy homeostasis and metabolism from the simplest to most complex organisms. We report a 1.5 A x-ray crystal structure of the first identified outer mitochondrial membrane Fe-S protein, mitoNEET. Two protomers intertwine to form a unique dimeric structure that constitutes a new fold to not only the approximately 650 reported Fe-S protein structures but also to all known proteins. We name this motif the NEET fold. The protomers form a two-domain structure: a beta-cap domain and a cluster-binding domain that coordinates two acid-labile 2Fe-2S clusters. Binding of pioglitazone, an insulin-sensitizing thiazolidinedione used in the treatment of type 2 diabetes, stabilizes the protein against 2Fe-2S cluster release. The biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe-S cluster transfer.
journal_name
Proc Natl Acad Sci U S Aauthors
Paddock ML,Wiley SE,Axelrod HL,Cohen AE,Roy M,Abresch EC,Capraro D,Murphy AN,Nechushtai R,Dixon JE,Jennings PAdoi
10.1073/pnas.0707189104subject
Has Abstractpub_date
2007-09-04 00:00:00pages
14342-7issue
36eissn
0027-8424issn
1091-6490pii
0707189104journal_volume
104pub_type
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