2QH7: Mitoneet IS a Uniquely Folded 2fe-2s Outer Mitochondrial Membrane Protein Stabilized by Pioglitazone

Citation:
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.
PDB ID: 2QH7Download
MMDB ID: 59466
PDB Deposition Date: 2007/6/30
Updated in MMDB: 2007/10 
Experimental Method:
x-ray diffraction
Resolution: 1.5  Å
Source Organism:
Similar Structures:
Biological Unit for 2QH7: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2QH7
Label Count Molecule
Proteins (2 molecules)
2
Zinc Finger Cdgsh-type Domain 1
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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