Reference: Hamburger ZA, et al. (2006) Crystal structure of the S.cerevisiae exocyst component Exo70p. J Mol Biol 356(1):9-21

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Abstract

The exocyst is an evolutionarily conserved multiprotein complex required for the targeting and docking of post-Golgi vesicles to the plasma membrane. Through its interactions with a variety of proteins, including small GTPases, the exocyst is thought to integrate signals from the cell and signal that vesicles arriving at the plasma membrane are ready for fusion. Here we describe the three-dimensional crystal structure of one of the components of the exocyst, Exo70p, from Saccharomyces cerevisae at 3.5A resolution. Exo70p binds the small GTPase Rho3p in a GTP-dependent manner with an equilibrium dissociation constant of approximately 70muM. Exo70p is an extended rod approximately 155A in length composed principally of alpha helices, and is a novel fold. The structure provides a first view of the Exo70 protein family and provides a framework to study the molecular function of this exocyst component.

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Journal Article
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Hamburger ZA, Hamburger AE, West AP Jr, Weis WI
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