2QH7
MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone
Summary for 2QH7
| Entry DOI | 10.2210/pdb2qh7/pdb |
| Descriptor | Zinc finger CDGSH-type domain 1, FE2/S2 (INORGANIC) CLUSTER (3 entities in total) |
| Functional Keywords | mitoneet, 2fe-2s protein, outer mitochrodrial membrane protein, pioglitazone binding, metal binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 18248.29 |
| 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 citation | 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. 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: 17766440DOI: 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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