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J. Biol. Chem., Vol. 280, Issue 16, 15960-15966, April 22, 2005

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Crystal Structure of a PhoU Protein Homologue

A NEW CLASS OF METALLOPROTEIN CONTAINING MULTINUCLEAR IRON CLUSTERS^*

Jinyu Liu, Yun Lou, Hisao Yokota, Paul D. Adams, Rosalind Kim, and Sung-Hou Kim¶

From the Berkeley Structural Genomics Center, Lawrence Berkeley National Laboratory, Berkeley, California 94720 and Department of Chemistry, University of California, Berkeley, California 94720-5230

PhoU proteins are known to play a role in the regulation of phosphate uptake. In Thermotoga maritima, two PhoU homologues have been identified bioinformatically. Here we report the crystal structure of one of the PhoU homologues at 2.0 Å resolution. The structure of the PhoU protein homologue contains a highly symmetric new structural fold composed of two repeats of a three-helix bundle. The structure unexpectedly revealed a trinuclear and a tetranuclear iron cluster that were found to be bound on the surface. Each of the two multinuclear iron clusters is coordinated by a conserved E(D)XXXD motif pair. Our structure reveals a new class of metalloprotein containing multinuclear iron clusters. The possible functional implication based on the structure are discussed.

Received for publication, December 15, 2004 , and in revised form, February 11, 2005.

^* This work was supported by the National Institutes of Health Grant GM 62412. 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 1SUM) 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 should be addressed. Fax: 510-486-5272; E-mail: SHKim{at}cchem.berkeley.edu.

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