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J. Biol. Chem., Vol. 279, Issue 45, 46787-46793, November 5, 2004

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Solution Structure of a Ubiquitin-like Domain from Tubulin-binding Cofactor B^*

Betsy L. Lytle, Francis C. Peterson, Shi-Hong Qiu¶, Ming Luo¶, Qin Zhao||, John L. Markley||, and Brian F. Volkman**

From the Center for Eukaryotic Structural Genomics, Madison, Wisconsin 53706-1549, Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, ^¶Center for Biophysical Sciences and Engineering, Southeast Collaboratory for Structural Genomics, University of Alabama at Birmingham, Birmingham, Alabama 35294, and ^||Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706

Proper folding and assembly of tubulin -heterodimers involves a stepwise progression mediated by a group of protein cofactors A through E. Upon release of the tubulin monomers from the chaperonin CCT, they are acted upon by each cofactor in the folding pathway through a unique combination of protein interaction domains. Three-dimensional structures have previously been reported for cofactor A and the C-terminal CAP-Gly domain of cofactor B (CoB). Here we report the NMR structure of the N-terminal domain of Caenorhabditis elegans CoB and show that it closely resembles ubiquitin as was recently postulated on the basis of bioinformatic analysis (Grynberg, M., Jaroszewski, L., and Godzik, A. (2003) BMC Bioinformatics 4, 46). CoB binds partially folded -tubulin monomers, and a putative tubulin-binding motif within the N-terminal domain is identified from sequence and structure comparisons. Based on modeling of the homologous cofactor E ubiquitin-like domain, we hypothesize that cofactors B and E may associate via their -grasp domains in a manner analogous to the PB1 and caspase-activated deoxyribonuclease superfamily of protein interaction domains.

Received for publication, August 17, 2004 , and in revised form, September 2, 2004.

^* This work was supported by the National Institutes of Health Protein Structure Initiative through Grant 1 P50 GM64598. 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 1T0Y) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

All time-domain NMR data and chemical shift assignments have been deposited in BioMagResBank (www.bmrb.wisc.edu/) under BMRB accession number 6176.

^** To whom correspondence should be addressed. Tel.: 414-456-8400; Fax: 414-456-6510; E-mail: bvolkman{at}mcw.edu.

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