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Originally published In Press as doi:10.1074/jbc.M008501200 on October 25, 2000

J. Biol. Chem., Vol. 276, Issue 4, 2786-2789, January 26, 2001
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Adrenodoxin Reductase-Adrenodoxin Complex Structure Suggests Electron Transfer Path in Steroid Biosynthesis*

Jürgen J. MüllerDagger §, Anna LapkoDagger , Gleb Bourenkov||, Klaus RuckpaulDagger , and Udo HeinemannDagger **Dagger Dagger

From Dagger  Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, D-13125 Berlin, || MPG-ASMB, c/o DESY, Notkestrasse 85, D-22603 Hamburg, and ** Institut für Chemie-Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195 Berlin, Germany

The steroid hydroxylating system of adrenal cortex mitochondria consists of the membrane-attached NADPH-dependent adrenodoxin reductase (AR), the soluble one-electron transport protein adrenodoxin (Adx), and a membrane-integrated cytochrome P450 of the CYP11 family. In the 2.3-Å resolution crystal structure of the Adx·AR complex, 580 Å2 of partly polar surface are buried. Main interaction sites are centered around Asp79, Asp76, Asp72, and Asp39 of Adx and around Arg211, Arg240, Arg244, and Lys27 of AR, respectively. In particular, the region around Asp39 defines a new protein interaction site for Adx, similar to those found in plant and bacterial ferredoxins. Additional contacts involve the electron transfer region between the redox centers of AR and Adx and C-terminal residues of Adx. The Adx residues Asp113 to Arg115 adopt 310-helical conformation and engage in loose intermolecular contacts within a deep cleft of AR. Complex formation is accompanied by a slight domain rearrangement in AR. The [2Fe-2S] cluster of Adx and the isoalloxazine rings of FAD of AR are 10 Å apart suggesting a possible electron transfer route between these redox centers. The AR·Adx complex represents the first structure of a biologically relevant complex between a ferredoxin and its reductase.


* This work was supported by Deutsche Forschungsgemeinschaft Grants He 1318/19-1 and WER436 and the Fonds der Chemischen Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The 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 the structure factors (code 1e6e) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ To whom correspondence may be addressed. Tel.: 49 30 9406 3421; E-mail: JJM@MDC-Berlin.de.

On leave from the International Sakharow Institute of Radioecology, 2220009 Minsk, Belarus.

Dagger Dagger To whom correspondence may be addressed. Tel.: 49 30 9406-3420; E-mail: Heinemann@MDC-Berlin.de.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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