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 a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a 160-A-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods.
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif.,Dong G, Hutagalung AH, Fu C, Novick P, Reinisch KM Nat Struct Mol Biol. 2005 Dec;12(12):1094-100. Epub 2005 Oct 26. PMID:16249794[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
- ↑ Dong G, Hutagalung AH, Fu C, Novick P, Reinisch KM. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol. 2005 Dec;12(12):1094-100. Epub 2005 Oct 26. PMID:16249794 doi:10.1038/nsmb1017
