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J. Biol. Chem., Vol. 281, Issue 27, 18746-18752, July 7, 2006

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The Structure of the Human Centrin 2-Xeroderma Pigmentosum Group C Protein Complex^*

James R. Thompson¹, Zachary C. Ryan, Jeffrey L. Salisbury^¶, and Rajiv Kumar^¶||

From the Departments of Physiology and Biomedical Engineering, ^||Medicine, and ^¶Biochemistry and Molecular Biology and the Mayo Proteomics Research Center, Mayo Clinic College of Medicine, Rochester, Minnesota 55905

Human centrin-2 plays a key role in centrosome function and stimulates nucleotide excision repair by binding to the xeroderma pigmentosum group C protein. To determine the structure of human centrin-2 and to develop an understanding of molecular interactions between centrin and xeroderma pigmentosum group C protein, we characterized the crystal structure of calcium-loaded full-length centrin-2 complexed with a xeroderma pigmentosum group C peptide. Our structure shows that the carboxyl-terminal domain of centrin-2 binds this peptide and two calcium atoms, whereas the amino-terminal lobe is in a closed conformation positioned distantly by an ordered -helical linker. A stretch of the amino-terminal domain unique to centrins appears disordered. Two xeroderma pigmentosum group C peptides both bound to centrin-2 also interact to form an -helical coiled-coil. The interface between centrin-2 and each peptide is predominantly nonpolar, and key hydrophobic residues of XPC have been identified that lead us to propose a novel binding motif for centrin.

Received for publication, December 22, 2005 , and in revised form, March 24, 2006.

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

^* This work was supported in part by the Mayo Clinic Foundation and National Institutes of Health Grants DK58546 and DK65830 (to R. K.). 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 on-line version of this article (available at http://www.jbc.org) contains a sequence alignment.

¹ To whom correspondence should be addressed: Mayo Clinic, 200 First St., SW, Rochester, MN 55905. Tel.: 507-538-3891; Fax: 507-538-3954; E-mail: thompson.james{at}mayo.edu.

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