The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Pharmacology
Life Sciences | Medicine and Health Sciences
The exocyst is a conserved protein complex essential for trafficking secretory vesicles to the plasma membrane. The structure of the C-terminal domain of the exocyst subunit Sec6p reveals multiple helical bundles, which are structurally and topologically similar to Exo70p and the C-terminal domains of Exo84p and Sec15, despite <10% sequence identity. The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins.
DOI of Published Version
Nat Struct Mol Biol. 2006 Jun;13(6):555-6. Epub 2006 May 14. Link to article on publisher's site
Nature structural and molecular biology
Sivaram, Mylavarapu V. S.; Furgason, Melonnie Lynn Marie; Brewer, Daniel Niron; and Munson, Mary, "The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles" (2006). GSBS Student Publications. 1122.