Structural highlights
Function
EXO70_YEAST Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in the assembly of the exocyst.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 cerevisiae at 3.5A resolution. Exo70p binds the small GTPase Rho3p in a GTP-dependent manner with an equilibrium dissociation constant of approximately 70 microM. Exo70p is an extended rod approximately 155 angstroms 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.
Crystal structure of the S.cerevisiae exocyst component Exo70p.,Hamburger ZA, Hamburger AE, West AP Jr, Weis WI J Mol Biol. 2006 Feb 10;356(1):9-21. Epub 2005 Nov 10. PMID:16359701[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wiederkehr A, De Craene JO, Ferro-Novick S, Novick P. Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p. J Cell Biol. 2004 Dec 6;167(5):875-87. PMID:15583030 doi:http://dx.doi.org/jcb.200408001
- ↑ Hamburger ZA, Hamburger AE, West AP Jr, Weis WI. Crystal structure of the S.cerevisiae exocyst component Exo70p. J Mol Biol. 2006 Feb 10;356(1):9-21. Epub 2005 Nov 10. PMID:16359701 doi:10.1016/j.jmb.2005.09.099
