Summary for 3C98
Entry DOI | 10.2210/pdb3c98/pdb |
Related | 1DN1 |
Descriptor | Syntaxin-binding protein 1, Syntaxin-1A (3 entities in total) |
Functional Keywords | protein complex, alternative splicing, cytoplasm, membrane, phosphoprotein, protein transport, transport, coiled coil, neurotransmitter transport, transmembrane, endocytosis-exocytosis complex, endocytosis/exocytosis |
Biological source | Rattus norvegicus (Norway rat) More |
Cellular location | Cytoplasm: P61765 Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851 |
Total number of polymer chains | 2 |
Total formula weight | 101522.69 |
Authors | Hattendorf, D.A.,Misura, K.M.,Burkhardt, P.,Scheller, R.H.,Fasshauer, D.,Weis, W.I. (deposition date: 2008-02-15, release date: 2008-03-25, Last modification date: 2024-03-13) |
Primary citation | Burkhardt, P.,Hattendorf, D.A.,Weis, W.I.,Fasshauer, D. Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide Embo J., 27:923-933, 2008 Cited by PubMed Abstract: Sec1/Munc18-like (SM) proteins functionally interact with SNARE proteins in vesicular fusion. Despite their high sequence conservation, structurally disparate binding modes for SM proteins with syntaxins have been observed. Several SM proteins appear to bind only to a short peptide present at the N terminus of syntaxin, designated the N-peptide, while Munc18a binds to a 'closed' conformation formed by the remaining portion of syntaxin 1a. Here, we show that the syntaxin 16 N-peptide binds to the SM protein Vps45, but the remainder of syntaxin 16 strongly enhances the affinity of the interaction. Likewise, the N-peptide of syntaxin 1a serves as a second binding site in the Munc18a/syntaxin 1a complex. When the syntaxin 1a N-peptide is bound to Munc18a, SNARE complex formation is blocked. Removal of the N-peptide enables binding of syntaxin 1a to its partner SNARE SNAP-25, while still bound to Munc18a. This suggests that Munc18a controls the accessibility of syntaxin 1a to its partners, a role that might be common to all SM proteins. PubMed: 18337752DOI: 10.1038/emboj.2008.37 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.601 Å) |
Structure validation
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