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J. Biol. Chem., Vol. 282, Issue 46, 33242-33246, November 16, 2007

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Crystallographic Studies of Human MitoNEET^*

Xiaowei Hou, Rujuan Liu^¶, Stuart Ross^¶||, Eric J. Smart^||, Haining Zhu^¶1, and Weimin Gong²

From the National Key Laboratory of Macrobiomolecule, Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P. R. China, the School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, P. R. China, the ^¶Department of Molecular and Cellular Biochemistry and the ^||Kentucky Pediatric Research Institute, Department of Pediatrics, College of Medicine, University of Kentucky, Lexington, Kentucky 40536-0509

MitoNEET was identified as an outer mitochondrial membrane protein that can potentially bind the anti-diabetes drug pioglitazone. The crystal structure of the cytoplasmic mitoNEET (residues 33–108) is determined in this study. The structure presents a novel protein fold and contains a [2Fe-2S] cluster-binding domain. The [2Fe-2S] cluster is coordinated to the protein by Cys-72, Cys-74, Cys-83, and His-87 residues. This coordination is also novel compared with the traditional [2Fe-2S] cluster coordinated by four cysteines or two cysteines and two histidines. The cytoplasmic mitoNEET forms homodimers in solution and in crystal. The dimerization is mainly mediated by hydrophobic interactions as well as hydrogen bonds coordinated by two water molecules binding at the interface. His-87 residue, which plays an important role in the coordination of the [2Fe-2S] cluster, is exposed to the solvent on the dimer surface. It is proposed that mitoNEET dimer may interact with other proteins via the surface residues in close proximity to the [2Fe-2S] cluster.

Received for publication, August 23, 2007 , and in revised form, September 24, 2007.

Addendum—After the submission of this manuscript, two groups published the crystal structure of the cytoplasmic portion of mitoNEET independently (37, 38).

^* This work was supported by the National Funding for Talent Youth Grant 30225015, the Ministry of Science and Technology Grants 2004CB720008, 2006CB0D1705, and 2007CB914304, the 863 program Grant 2006AA02A316, the National Natural Science Foundation of China Grants 10490193 and 30728004 and the Chinese Academy of Sciences Grant KSCX2-YW-R-61 (to W. G.) and by National Institutes of Health Grants R01 DK077632 and P20RR015592 (to E. J. S.) and R01NS049126 (to H. Z.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (code 2R13) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

¹ To whom correspondence may be addressed: Dept. of Molecular and Cellular Biochemistry, University of Kentucky, 741 South Limestone, Lexington, KY 40536-0509. E-mail: haining{at}uky.edu. ² To whom correspondence may be addressed. E-mail: wgong{at}ibp.ac.cn.

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