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J. Biol. Chem., Vol. 282, Issue 32, 23418-23426, August 10, 2007

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Structural Analysis of Conserved Oligomeric Golgi Complex Subunit 2^*

Lorraine F. Cavanaugh¹, Xiaocheng Chen, Brian C. Richardson, Daniel Ungar, Istvan Pelczer^¶, Josep Rizo, and Frederick M. Hughson²

From the Departments of Molecular Biology and ^¶Chemistry, Princeton University, Princeton, New Jersey 08544 and the Departments of Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390

The conserved oligomeric Golgi (COG) complex is strongly implicated in retrograde vesicular trafficking within the Golgi apparatus. Although its mechanism of action is poorly understood, it has been proposed to function by mediating the initial physical contact between transport vesicles and their membrane targets. An analogous role in tethering vesicles has been suggested for at least six additional large multisubunit complexes, including the exocyst, a complex essential for trafficking to the plasma membrane. Here we report the solution structure of a large portion of yeast Cog2p, one of eight subunits composing the COG complex. The structure reveals a six-helix bundle with few conserved surface features but a general resemblance to recently determined crystal structures of four different exocyst subunits. This finding provides the first structural evidence that COG, like the exocyst and potentially other tethering complexes, is constructed from helical bundles. These structures may represent platforms for interaction with other trafficking proteins including SNAREs (soluble N-ethylmaleimide factor attachment protein receptors) and Rabs.

Received for publication, May 4, 2007 , and in revised form, June 7, 2007.

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

Experimental NMR chemical shift and restraint data have been deposited in the Biological Magnetic Resonance Data Bank (www.bmrb.wisc.edu) with the accession number 15290.

^* This work was supported by a National Science Foundation Minority Postdoctoral Fellowship (to L. F. C.), by an American Heart Association grant-in-aid (to F. M. H.), and by National Institutes of Health Grants GM071574 (to F. M. H.) and NS37200 (to J. R.). 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.

¹ Current address: Department of Biological Sciences, Columbia University, New York, NY 10027.

² To whom correspondence should be addressed. Tel.: 609-258-4982; Fax: 609-258-6730; E-mail: hughson{at}princeton.edu.

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