3B5N

Structure of the yeast plasma membrane SNARE complex

Summary for 3B5N

• Entry DOI: 10.2210/pdb3b5n/pdb
• Descriptor: Synaptobrevin homolog 1, Protein SSO1, Protein transport protein SEC9, ... (5 entities in total)
• Functional Keywords: snare complex, syntaxin, synaptobrevin, snap-25, sso1p, snc1p, sec9p, sec9, sso1, snc1, coiled coil, lipoprotein, membrane, palmitate, transmembrane, ubl conjugation, phosphorylation, protein transport, transport, membrane protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Endomembrane system; Single-pass type IV membrane protein: P31109; Membrane ; Single-pass type IV membrane protein : P32867
• Total number of polymer chains: 12
• Total formula weight: 88812.68

Authors

Strop, P.,Brunger, A.T. (deposition date: 2007-10-26, release date: 2007-11-20, Last modification date: 2023-08-30)

Primary citation

Strop, P.,Kaiser, S.E.,Vrljic, M.,Brunger, A.T.
The Structure of the Yeast Plasma Membrane SNARE Complex Reveals Destabilizing Water-filled Cavities.
J.Biol.Chem., 283:1113-1119, 2008

PubMed Abstract: 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.

PubMed: 17956869
DOI: 10.1074/jbc.M707912200

Experimental method

X-RAY DIFFRACTION (1.6 Å)