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| | ==Lipid-induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6== | | ==Lipid-induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6== |
| - | <StructureSection load='3kyq' size='340' side='right' caption='[[3kyq]], [[Resolution|resolution]] 2.44Å' scene=''> | + | <StructureSection load='3kyq' size='340' side='right'caption='[[3kyq]], [[Resolution|resolution]] 2.44Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3kyq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KYQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3kyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KYQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.443Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ykt6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3kyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kyq OCA], [http://pdbe.org/3kyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kyq RCSB], [http://www.ebi.ac.uk/pdbsum/3kyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kyq ProSAT]</span></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=3kyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kyq OCA], [https://pdbe.org/3kyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kyq RCSB], [https://www.ebi.ac.uk/pdbsum/3kyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kyq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YKT6_RAT YKT6_RAT]] Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity.<ref>PMID:11323436</ref> | + | [https://www.uniprot.org/uniprot/YKT6_RAT YKT6_RAT] Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity.<ref>PMID:11323436</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Wen, W Y]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Yu, J]] | + | [[Category: Wen WY]] |
| - | [[Category: Zhang, M J]] | + | [[Category: Yu J]] |
| - | [[Category: Cytoplasmic vesicle]] | + | [[Category: Zhang MJ]] |
| - | [[Category: Er-golgi transport]]
| + | |
| - | [[Category: Golgi apparatus]]
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| - | [[Category: Lipid binding]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Palmitate]]
| + | |
| - | [[Category: Prenylation]]
| + | |
| - | [[Category: Protein transport]]
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| - | [[Category: Transferase]]
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| - | [[Category: Transport]]
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| - | [[Category: V-snare homolog]]
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| Structural highlights
Function
YKT6_RAT Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity.[1]
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
While most SNAREs are permanently anchored to membranes by their transmembrane domains, the dually lipidated SNARE Ykt6 is found both on intracellular membranes and in the cytosol. The cytosolic Ykt6 is inactive due to the autoinhibition of the SNARE core by its longin domain, although the molecular basis of this inhibition is unknown. Here, we demonstrate that unlipidated Ykt6 adopts multiple conformations, with a small population in the closed state. The structure of Ykt6 in complex with a fatty acid suggests that, upon farnesylation, the Ykt6 SNARE core forms four alpha helices that wrap around the longin domain, forming a dominantly closed conformation. The fatty acid, buried in a hydrophobic groove formed between the longin domain and its SNARE core, is essential for maintaining the autoinhibited conformation of Ykt6. Our study reveals that the posttranslationally attached farnesyl group can actively regulate Ykt6 fusion activity in addition to its anticipated membrane-anchoring role.
Lipid-Induced conformational switch controls fusion activity of longin domain SNARE Ykt6.,Wen W, Yu J, Pan L, Wei Z, Weng J, Wang W, Ong YS, Tran TH, Hong W, Zhang M Mol Cell. 2010 Feb 12;37(3):383-95. PMID:20159557[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang T, Hong W. Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport. J Biol Chem. 2001 Jul 20;276(29):27480-7. Epub 2001 Apr 25. PMID:11323436 doi:http://dx.doi.org/10.1074/jbc.M102786200
- ↑ Wen W, Yu J, Pan L, Wei Z, Weng J, Wang W, Ong YS, Tran TH, Hong W, Zhang M. Lipid-Induced conformational switch controls fusion activity of longin domain SNARE Ykt6. Mol Cell. 2010 Feb 12;37(3):383-95. PMID:20159557 doi:10.1016/j.molcel.2010.01.024
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