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2QH7

MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone

Summary for 2QH7
Entry DOI10.2210/pdb2qh7/pdb
DescriptorZinc finger CDGSH-type domain 1, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
Functional Keywordsmitoneet, 2fe-2s protein, outer mitochrodrial membrane protein, pioglitazone binding, metal binding protein
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight18248.29
Authors
Paddock, M.L.,Wiley, S.E.,Axelrod, H.L.,Cohen, A.E.,Roy, M.,Abresch, E.C.,Capraro, D.,Murphy, A.N.,Nechushtai, R.,Dixon, J.E.,Jennings, P.A. (deposition date: 2007-06-30, release date: 2007-08-21, Last modification date: 2024-02-21)
Primary citationPaddock, M.L.,Wiley, S.E.,Axelrod, H.L.,Cohen, A.E.,Roy, M.,Abresch, E.C.,Capraro, D.,Murphy, A.N.,Nechushtai, R.,Dixon, J.E.,Jennings, P.A.
MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone.
Proc.Natl.Acad.Sci.Usa, 104:14342-14347, 2007
Cited by
PubMed 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.
PubMed: 17766440
DOI: 10.1073/pnas.0707189104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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