1hs7
From Proteopedia
(New page: 200px<br /><applet load="1hs7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hs7" /> '''VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE''...) |
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| - | [[Image:1hs7.gif|left|200px]]<br /><applet load="1hs7" size=" | + | [[Image:1hs7.gif|left|200px]]<br /><applet load="1hs7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hs7" /> | caption="1hs7" /> | ||
'''VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE'''<br /> | '''VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Syntaxins and Sec1/munc18 proteins are central to intracellular membrane | + | 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== | ==About this Structure== | ||
| - | 1HS7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1HS7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HS7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dulubova, I.]] | [[Category: Dulubova, I.]] | ||
[[Category: Rizo, J.]] | [[Category: Rizo, J.]] | ||
| - | [[Category: Sudhof, T | + | [[Category: Sudhof, T C.]] |
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
[[Category: Yamaguchi, T.]] | [[Category: Yamaguchi, T.]] | ||
[[Category: up-and-down three-helix bundle insertion preceding proline in an alpha-helix]] | [[Category: up-and-down three-helix bundle insertion preceding proline in an alpha-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:20 2008'' |
Revision as of 11:04, 21 February 2008
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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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