1PD0

Crystal structure of the COPII coat subunit, Sec24, complexed with a peptide from the SNARE protein Sed5 (yeast syntaxin-5)

Summary for 1PD0

• Entry DOI: 10.2210/pdb1pd0/pdb
• Related: 1PCX 1PD1
• Descriptor: Protein transport protein Sec24, COPII-binding peptide of the integral membrane protein SED5, ZINC ION, ... (4 entities in total)
• Functional Keywords: transport protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm: P40482; Membrane; Single-pass type IV membrane protein (Potential): Q01590
• Total number of polymer chains: 2
• Total formula weight: 92095.35

Authors

Mossessova, E.,Bickford, L.C.,Goldberg, J. (deposition date: 2003-05-18, release date: 2003-08-19, Last modification date: 2024-02-14)

Primary citation

Mossessova, E.,Bickford, L.C.,Goldberg, J.
SNARE selectivity of the COPII coat.
Cell(Cambridge,Mass.), 114:483-495, 2003

PubMed Abstract: The COPII coat buds transport vesicles from the endoplasmic reticulum that incorporate cargo and SNARE molecules. Here, we show that recognition of the ER-Golgi SNAREs Bet1, Sed5, and Sec22 occurs through three binding sites on the Sec23/24 subcomplex of yeast COPII. The A site binds to the YNNSNPF motif of Sed5. The B site binds to Lxx-L/M-E sequences present in both the Bet1 and Sed5 molecules, as well as to the DxE cargo-sorting signal. A third, spatially distinct site binds to Sec22. COPII selects the free v-SNARE form of Bet1 because the LxxLE sequence is sequestered in the four-helix bundle of the v-/t-SNARE complex. COPII favors Sed5 within the Sed5/Bos1/Sec22 t-SNARE complex because t-SNARE assembly removes autoinhibitory contacts to expose the YNNSNPF motif. The COPII coat seems to be a specific conductor of the fusogenic forms of these SNAREs, suggesting how vesicle fusion specificity may be programmed during budding.

PubMed: 12941276
DOI: 10.1016/S0092-8674(03)00608-1

Experimental method

X-RAY DIFFRACTION (2.6 Å)