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J. Biol. Chem., Vol. 278, Issue 36, 34373-34379, September 5, 2003

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The Structure of Aip1p, a WD Repeat Protein That Regulates Cofilin-mediated Actin Depolymerization^*

Walter C. Voegtli, A. Yarrow Madrona and David K. Wilson 

From the Section of Molecular and Cellular Biology, University of California, Davis, California 95616

Actin-interacting protein 1 (Aip1p) is a 67-kDa WD repeat protein known to regulate the depolymerization of actin filaments by cofilin and is conserved in organisms ranging from yeast to mammals. The crystal structure of Aip1p from Saccharomyces cerevisiae was determined to a 2.3-Å resolution and a final crystallographic R-factor of 0.204. The structure reveals that the overall fold is formed by two connected seven-bladed -propellers and has important implications for the structure of Aip1 from other organisms and WD repeat-containing proteins in general. These results were unexpected because a maximum of 10 WD repeats had been reported in the literature for this protein using sequence data. The surfaces of the -propellers formed by the D-A and B-C loops are positioned adjacent to one another, giving Aip1p a shape that resembles an open "clamshell." The mapping of conserved residues to the structure of Aip1p reveals dense patches of conserved residues on the surface of one -propeller and at the interface of the two -propellers. These two patches of conserved residues suggest a potential binding site for F-actin on Aip1p and that the orientation of the -propellers with respect to one another plays a role in binding an actin-cofilin complex. In addition, the conserved interface between the domains is mediated by a number of interactions that appear to impart rigidity between the two domains of Aip1p and may make a large substrate-induced conformational change difficult.

Received for publication, March 18, 2003 , and in revised form, June 4, 2003.

The atomic coordinates and structure factors (code 1PI6 for native Aip1p and 1PGU for Se-Met-Aip1p) 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 by Grant GM66135 from the National Institutes of Health (to D. K. W.) and the Keck Foundation. The data collection facilities at Stanford Synchrotron Radiation Laboratory are funded by the U. S. Department of Energy and the National Institutes of Health. 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.

To whom correspondence should be addressed: Section of Molecular and Cellular Biology, One Shields Ave., University of California, Davis, CA 95616. Tel.: 530-752-1136; Fax: 530-752-3085; E-mail: dave{at}alanine.ucdavis.edu.

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