3kyq

From Proteopedia

(Difference between revisions)

Revision as of 07:23, 2 January 2019

Lipid-induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6

Structural highlights

3kyq is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	Ykt6 (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3kyq"

@@ Line 1: / Line 1: @@
 ==Lipid-induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6==
 <StructureSection load='3kyq' size='340' side='right' caption='[[3kyq]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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>
 <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='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]</span></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>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/3kyq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/3kyq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3kyq

From Proteopedia

Revision as of 07:23, 2 January 2019

Lipid-induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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