2FJI

Crystal structure of the C-terminal domain of the exocyst subunit Sec6p

Summary for 2FJI

• Entry DOI: 10.2210/pdb2fji/pdb
• Descriptor: Exocyst complex component SEC6 (2 entities in total)
• Functional Keywords: exocyst complex, exocytosis, tandem helical bundles, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P32844
• Total number of polymer chains: 2
• Total formula weight: 92501.44

Authors

Sivaram, M.V.,Munson, M. (deposition date: 2006-01-02, release date: 2006-05-16, Last modification date: 2024-02-14)

Primary citation

Sivaram, M.V.,Furgason, M.L.,Brewer, D.N.,Munson, M.
The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles.
Nat.Struct.Mol.Biol., 13:555-556, 2006

PubMed 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.

PubMed: 16699513
DOI: 10.1038/nsmb1096

Experimental method

X-RAY DIFFRACTION (2.4 Å)