Structural highlights
FunctionSNC1_YEAST SNC1 and SNC2 are vesicle-targeting proteins essential for normal secretory traffic between the Golgi and the plasma membrane. They may also be involved in vesicle fusion. 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 PubMedSNARE proteins form a complex that leads to membrane fusion between vesicles, organelles, and plasma membrane in all eukaryotic cells. We report the 1.7A resolution structure of the SNARE complex that mediates exocytosis at the plasma membrane in the yeast Saccharomyces cerevisiae. Similar to its neuronal and endosomal homologues, the S. cerevisiae SNARE complex forms a parallel four-helix bundle in the center of which is an ionic layer. The S. cerevisiae SNARE complex exhibits increased helix bending near the ionic layer, contains water-filled cavities in the complex core, and exhibits reduced thermal stability relative to mammalian SNARE complexes. Mutagenesis experiments suggest that the water-filled cavities contribute to the lower stability of the S. cerevisiae complex. The structure of the yeast plasma membrane SNARE complex reveals destabilizing water-filled cavities.,Strop P, Kaiser SE, Vrljic M, Brunger AT J Biol Chem. 2008 Jan 11;283(2):1113-9. Epub 2007 Oct 22. PMID:17956869[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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