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3C98

Revised structure of the munc18a-syntaxin1 complex

Replaces:  1DN1
Summary for 3C98
Entry DOI10.2210/pdb3c98/pdb
Related1DN1
DescriptorSyntaxin-binding protein 1, Syntaxin-1A (3 entities in total)
Functional Keywordsprotein complex, alternative splicing, cytoplasm, membrane, phosphoprotein, protein transport, transport, coiled coil, neurotransmitter transport, transmembrane, endocytosis-exocytosis complex, endocytosis/exocytosis
Biological sourceRattus norvegicus (Norway rat)
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Cellular locationCytoplasm: P61765
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851
Total number of polymer chains2
Total formula weight101522.69
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 citationBurkhardt, 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: 18337752
DOI: 10.1038/emboj.2008.37
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.601 Å)
Structure validation

239803

数据于2025-08-06公开中

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