Structural highlights
Function
[SEC3_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 an evolutionarily conserved octameric complex involved in polarized exocytosis from yeast to humans. The Sec3 subunit of the exocyst acts as a spatial landmark for exocytosis through its ability to bind phospholipids and small GTPases. The structure of the N-terminal domain of Sec3 (Sec3N) was determined ab initio and defines a new subclass of pleckstrin homology (PH) domains along with a new family of proteins carrying this domain. Respectively, N- and C-terminal to the PH domain Sec3N presents an additional alpha-helix and two beta-strands that mediate dimerization through domain swapping. The structure identifies residues responsible for phospholipid binding, which when mutated in cells impair the localization of exocyst components at the plasma membrane and lead to defects in exocytosis. Through its ability to bind the small GTPase Cdc42 and phospholipids, the PH domain of Sec3 functions as a coincidence detector at the plasma membrane.
Structure-function study of the N-terminal domain of exocyst subunit Sec3.,Baek K, Knodler A, Lee SH, Zhang X, Orlando K, Zhang J, Foskett TJ, Guo W, Dominguez R J Biol Chem. 2010 Apr 2;285(14):10424-33. Epub 2010 Feb 5. PMID:20139078[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baek K, Knodler A, Lee SH, Zhang X, Orlando K, Zhang J, Foskett TJ, Guo W, Dominguez R. Structure-function study of the N-terminal domain of exocyst subunit Sec3. J Biol Chem. 2010 Apr 2;285(14):10424-33. Epub 2010 Feb 5. PMID:20139078 doi:10.1074/jbc.M109.096966
