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
Medical Subject Headings
Animals; Drosophila Proteins; Models, Molecular; Protein Conformation; Vesicular Transport Proteins
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.
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Citation: Nat Struct Mol Biol. 2006 Jun;13(6):555-6. Epub 2006 May 14. Link to article on publisher's site
DOI of Published Version
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.