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J. Biol. Chem., Vol. 280, Issue 23, 21981-21986, June 10, 2005

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Crystal Structure of Dynein Light Chain TcTex-1^*

John C. Williams¶, Hui Xie||, and Wayne A. Hendrickson**

From the Department of Biochemistry and Molecular Biophysics, the ^||Department of Pharmacology, and ^**Howard Hughes Medical Institute, Columbia University, New York, New York 10032

TcTex-1, one of three dynein light chains of the dynein motor complex, has been implicated in targeting and binding cargoes to cytoplasmic dynein for retrograde or apical transport. Interactions between TcTex-1 and a diverse set of proteins such as the dynein intermediate chain, Fyn, DOC2, FIP1, the poliovirus receptor, CD155, and the rhodopsin cytoplasmic tail have been reported; yet, despite the broad range of targets, a consensus binding sequence remains uncertain. Consequently, we have solved the crystal structure of the full-length Drosophila homolog of TcTex-1 to 1.7 Å resolution using MAD phasing to gain insight into its function and target specificity. The structure is homodimeric with a domain swapping of -strand 2 and has a fold similar to the dynein light chain, LC8. Based on structural alignment, the TcTex-1 and LC8 sequences show no identity, although the root mean square deviation between secondary structural elements is less than 1.6 Å. Moreover, the N terminus, which is equivalent to -strand 1 in LC8, is splayed out and binds to a crystallographic dimer as an anti-parallel -strand at the same position as the neuronal nitric-oxide synthase peptide in the LC8 complex. Similarity to LC8 and comparison to the LC8-neuronal nitricoxide synthase complex suggest that TcTex-1 binds its targets in a similar manner as LC8 and provides insight to the lack of strict sequence identity among the targets for TcTex-1.

Received for publication, December 29, 2004 , and in revised form, February 3, 2005.

^* This work was supported in part by a Career Development Award from the Leukemia and Lymphoma Society (to J. C. W.) and by National Institutes of Health Grant GM34102. 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 Figs. 1 and 2.

The atomic coordinates and structure factors (code 1YGT) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Both authors equally contributed to this work.

^¶ Present address: Kimmel Cancer Center, Thomas Jefferson University, 233 South 10th St., BLSB 826, Philadelphia, PA 19107.

To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biophysics, New York, NY 10032. Tel.: 212-305-1846; Fax: 212-305-7379; E-mail: wayne{at}convex.hhmi.columbia.edu.

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