Structural highlights
Function
[SEC6_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
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 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.
The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles.,Sivaram MV, Furgason ML, Brewer DN, Munson M Nat Struct Mol Biol. 2006 Jun;13(6):555-6. Epub 2006 May 14. PMID:16699513[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sivaram MV, Furgason ML, Brewer DN, Munson M. The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles. Nat Struct Mol Biol. 2006 Jun;13(6):555-6. Epub 2006 May 14. PMID:16699513 doi:10.1038/nsmb1096
