1hs7: Difference between revisions

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[[Image:1hs7.gif|left|200px]]


{{Structure
==VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE==
|PDB= 1hs7 |SIZE=350|CAPTION= <scene name='initialview01'>1hs7</scene>
<StructureSection load='1hs7' size='340' side='right'caption='[[1hs7]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|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>
[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.
}}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hs7" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Syntaxin 3D structures|Syntaxin 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Dulubova I]]
[[Category: Dulubova, I.]]
[[Category: Rizo J]]
[[Category: Rizo, J.]]
[[Category: Sudhof TC]]
[[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]]
 
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Retrieved from "https://proteopedia.org/1hs7"