1hs7: Difference between revisions

Line 1:

[[~~Image~~:1hs7.~~png|left|200px~~]]

==VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE==

== Structural highlights ==

<table><tr><td colspan='2'>[[1hs7]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HS7 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1hs7 RCSB], [http://www.ebi.ac.uk/pdbsum/1hs7 PDBsum]</span></td></tr>

<table>

== 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.

~~{{STRUCTURE_1hs7| PDB=1hs7 | SCENE= }}~~

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>

~~===VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_11224573}}~~

== References ==

~~==About this Structure==~~

__TOC__

~~[[1hs7]] is~~ a ~~1 chain structure with sequence from [http://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].~~

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:011224573<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Saccharomyces cerevisiae]]

[[Category: Dulubova, I.]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1hs7.png|left|200px]]
+==VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE==
+<StructureSection load='1hs7' size='340' side='right' caption='[[1hs7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hs7]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HS7 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1hs7 RCSB], [http://www.ebi.ac.uk/pdbsum/1hs7 PDBsum]</span></td></tr>
+<table>
+<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.
-{{STRUCTURE_1hs7|  PDB=1hs7  |  SCENE=  }}
+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>
-===VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11224573}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[1hs7]] is a 1 chain structure with sequence from [http://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].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:011224573</ref><references group="xtra"/>
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Dulubova, I.]]