1hs7

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hs7 OCA], [http://www.ebi.ac.uk/pdbsum/1hs7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hs7 RCSB]</span>
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[[Category: up-and-down three-helix bundle insertion preceding proline in an alpha-helix]]
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Revision as of 18:09, 30 March 2008


PDB ID 1hs7

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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