1HS7

VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE

Summary for 1HS7

• Entry DOI: 10.2210/pdb1hs7/pdb
• NMR Information: BMRB: 4945
• Descriptor: SYNTAXIN VAM3 (1 entity in total)
• Functional Keywords: up-and-down three-helix bundle insertion preceding proline in an alpha-helix, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Vacuole membrane; Single-pass type IV membrane protein: Q12241
• Total number of polymer chains: 1
• Total formula weight: 11354.98

Authors

Dulubova, I.,Yamaguchi, T.,Wang, Y.,Sudhof, T.C.,Rizo, J. (deposition date: 2000-12-24, release date: 2001-03-07, Last modification date: 2024-05-22)

Primary citation

Dulubova, I.,Yamaguchi, T.,Wang, Y.,Sudhof, T.C.,Rizo, J.
Vam3p structure reveals conserved and divergent properties of syntaxins.
Nat.Struct.Biol., 8:258-264, 2001

PubMed Abstract: Syntaxins and Sec1/munc18 proteins are central to intracellular membrane fusion. All syntaxins comprise a variable N-terminal region, a conserved SNARE motif that is critical for SNARE complex formation, and a transmembrane region. The N-terminal region of neuronal syntaxin 1A contains a three-helix domain that folds back onto the SNARE motif forming a 'closed' conformation; this conformation is required for munc18-1 binding. We have examined the generality of the structural properties of syntaxins by NMR analysis of Vam3p, a yeast syntaxin essential for vacuolar fusion. Surprisingly, Vam3p also has an N-terminal three-helical domain despite lacking apparent sequence homology with syntaxin 1A in this region. However, Vam3p does not form a closed conformation and its N-terminal domain is not required for binding to the Sec1/munc18 protein Vps33p, suggesting that critical distinctions exist in the mechanisms used by syntaxins to govern different types of membrane fusion.

PubMed: 11224573
DOI: 10.1038/85012

Experimental method

SOLUTION NMR