The Structure of the Yeast Plasma Membrane SNARE Complex Reveals Destabilizing Water-filled Cavities
| Autor: | Pavel Strop, Stephen E. Kaiser, Axel T. Brunger, Marija Vrljic |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins Protein Conformation Endosome Saccharomyces cerevisiae Endosomes Crystallography X-Ray Biochemistry Exocytosis R-SNARE Proteins Protein structure Animals Molecular Biology Neurons Binding Sites biology Vesicle Cell Membrane Water Lipid bilayer fusion Cell Biology biology.organism_classification Recombinant Proteins Cell biology Membrane protein Mutagenesis SNARE complex |
| Zdroj: | Journal of Biological Chemistry. 283:1113-1119 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m707912200 |
| Popis: | SNARE 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. |
| Databáze: | OpenAIRE |
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