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1hs7

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Revision as of 07:27, 7 April 2021

VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE

Structural highlights

1hs7 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

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 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^[1]

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

References

↑ Dulubova I, Yamaguchi T, Wang Y, Sudhof TC, Rizo J. Vam3p structure reveals conserved and divergent properties of syntaxins. Nat Struct Biol. 2001 Mar;8(3):258-64. PMID:11224573 doi:10.1038/85012

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hs7"

@@ Line 3: / Line 3: @@
 <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. 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>
+<table><tr><td colspan='2'>[[1hs7]] is a 1 chain structure. 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>
-</td></tr><tr id='resources'><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://pdbe.org/1hs7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hs7 RCSB], [http://www.ebi.ac.uk/pdbsum/1hs7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hs7 ProSAT]</span></td></tr>
+</td></tr><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>
 </table>
 == Function ==
-[[http://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.
+[[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 ==
@@ Line 19: / Line 19: @@
 ==See Also==
-*[[Syntaxin|Syntaxin]]
+*[[Syntaxin 3D structures|Syntaxin 3D structures]]
 == References ==
 <references/>

1hs7

From Proteopedia

Revision as of 07:27, 7 April 2021

VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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