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J. Biol. Chem., Vol. 276, Issue 4, 2786-2789, January 26, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/4/2786    most recent M008501200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Müller, J. J. Articles by Heinemann, U. Search for Related Content PubMed PubMed Citation Articles by Müller, J. J. Articles by Heinemann, U. Social Bookmarking                      What's this?

Adrenodoxin Reductase-Adrenodoxin Complex Structure Suggests Electron Transfer Path in Steroid Biosynthesis^*

Jürgen J. Müller^§, Anna Lapko^¶, Gleb Bourenkov, Klaus Ruckpaul, and Udo Heinemann^**

From  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.

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/).

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