1hs7
From Proteopedia
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VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE
Overview
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.
About this Structure
1HS7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Vam3p structure reveals conserved and divergent properties of syntaxins., Dulubova I, Yamaguchi T, Wang Y, Sudhof TC, Rizo J, Nat Struct Biol. 2001 Mar;8(3):258-64. PMID:11224573
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