1hs7

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[[Image:1hs7.gif|left|200px]]
 
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==VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE==
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The line below this paragraph, containing "STRUCTURE_1hs7", creates the "Structure Box" on the page.
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<StructureSection load='1hs7' size='340' side='right'caption='[[1hs7]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1hs7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HS7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hs7 OCA], [https://pdbe.org/1hs7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hs7 RCSB], [https://www.ebi.ac.uk/pdbsum/1hs7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hs7 ProSAT]</span></td></tr>
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{{STRUCTURE_1hs7| PDB=1hs7 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VAM3_YEAST VAM3_YEAST] Required for vacuolar assembly. Provides the t-SNARE function in a late step of the vacuolar assembly. Required for homotypic vacuole membrane fusion, autophagy and fusion of biosynthetic transport vesicles with the vacuole. Required for the delivery of alpha-factor receptor-ligand complexes to the vacuole.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE'''
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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<ref>PMID:11224573</ref>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1HS7 is a [[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].
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</div>
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<div class="pdbe-citations 1hs7" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11224573 11224573]
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*[[Syntaxin 3D structures|Syntaxin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Dulubova I]]
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[[Category: Dulubova, I.]]
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[[Category: Rizo J]]
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[[Category: Rizo, J.]]
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[[Category: Sudhof TC]]
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[[Category: Sudhof, T C.]]
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[[Category: Wang Y]]
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[[Category: Wang, Y.]]
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[[Category: Yamaguchi T]]
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[[Category: Yamaguchi, T.]]
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[[Category: Up-and-down three-helix bundle insertion preceding proline in an alpha-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:52 2008''
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Current revision

VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE

PDB ID 1hs7

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