title: The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA.
authors.forename: Mylavarapu V S
authors.initials: MV
authors.lastname: Sivaram
authors.forename: Melonnie L M
authors.initials: ML
authors.lastname: Furgason
authors.forename: Daniel N
authors.initials: DN
authors.lastname: Brewer
authors.forename: Mary
authors.initials: M
authors.lastname: Munson
mesh_terms: D000818:Animals; D029721:Drosophila Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D033921:Vesicular Transport Proteins / Q000737:chemistry*
chemical_list: D029721:Drosophila Proteins; C502606:Sec6 protein, Drosophila; D033921:Vesicular Transport Proteins