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| | <StructureSection load='1gl2' size='340' side='right'caption='[[1gl2]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1gl2' size='340' side='right'caption='[[1gl2]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gl2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gl2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GL2 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=1gl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl2 OCA], [http://pdbe.org/1gl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gl2 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl2 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1gl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl2 OCA], [https://pdbe.org/1gl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gl2 RCSB], [https://www.ebi.ac.uk/pdbsum/1gl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/VAMP8_RAT VAMP8_RAT] SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Also plays a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (PubMed:12737809). Involved in the homotypic fusion of early and late endosomes (PubMed:10982406, PubMed:11029036). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (By similarity).[UniProtKB:Q9BV40]<ref>PMID:10982406</ref> <ref>PMID:11029036</ref> <ref>PMID:12737809</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Syntaxin|Syntaxin]] | + | *[[Syntaxin 3D structures|Syntaxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Antonin, W]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Becker, S]] | + | [[Category: Antonin W]] |
| - | [[Category: Jahn, R]] | + | [[Category: Becker S]] |
| - | [[Category: Schneider, T R]] | + | [[Category: Jahn R]] |
| - | [[Category: Coiled coil]] | + | [[Category: Schneider TR]] |
| - | [[Category: Membrane fusion protein complex]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
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| Structural highlights
Function
VAMP8_RAT SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Also plays a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (PubMed:12737809). Involved in the homotypic fusion of early and late endosomes (PubMed:10982406, PubMed:11029036). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (By similarity).[UniProtKB:Q9BV40][1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
SNARE proteins are crucial for intracellular membrane fusion in all eukaryotes. These proteins assemble into tight complexes that connect membranes and may induce fusion. The crystal structure of the neuronal core complex is represented by an unusually long bundle of four alpha-helices connected by 16 layers of mostly hydrophobic amino acids. Here we report the 1.9 A resolution crystal structure of an endosomal SNARE core complex containing four SNAREs: syntaxin 7, syntaxin 8, vti1b and endobrevin/VAMP-8. Despite limited sequence homology, the helix alignment and the layer structure of the endosomal complex are remarkably similar to those of the neuronal complex. However, subtle variations are evident that characterize different SNARE subfamilies. We conclude that the structure of the SNARE core complex is an evolutionarily conserved hallmark of all SNARE complexes and is intimately associated with the general role of SNAREs in membrane fusion.
Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs.,Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR Nat Struct Biol. 2002 Feb;9(2):107-11. PMID:11786915[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mullock BM, Smith CW, Ihrke G, Bright NA, Lindsay M, Parkinson EJ, Brooks DA, Parton RG, James DE, Luzio JP, Piper RC. Syntaxin 7 is localized to late endosome compartments, associates with Vamp 8, and Is required for late endosome-lysosome fusion. Mol Biol Cell. 2000 Sep;11(9):3137-53. PMID:10982406
- ↑ Antonin W, Holroyd C, Tikkanen R, Höning S, Jahn R. The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes. Mol Biol Cell. 2000 Oct;11(10):3289-98. PMID:11029036 doi:10.1091/mbc.11.10.3289
- ↑ Low SH, Li X, Miura M, Kudo N, Quiñones B, Weimbs T. Syntaxin 2 and endobrevin are required for the terminal step of cytokinesis in mammalian cells. Dev Cell. 2003 May;4(5):753-9. PMID:12737809 doi:10.1016/s1534-5807(03)00122-9
- ↑ Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR. Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs. Nat Struct Biol. 2002 Feb;9(2):107-11. PMID:11786915 doi:http://dx.doi.org/10.1038/nsb746
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