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Crystal structure of the C-terminal domain of the exocyst subunit Sec6pCrystal structure of the C-terminal domain of the exocyst subunit Sec6p
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 PubMedThe 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
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