2c5k: Difference between revisions

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 <StructureSection load='2c5k' size='340' side='right'caption='[[2c5k]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c5k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C5K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c5k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C5K FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.05&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c5i|2c5i]], [[2c5j|2c5j]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2c5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5k OCA], [http://pdbe.org/2c5k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c5k RCSB], [http://www.ebi.ac.uk/pdbsum/2c5k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5k 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=2c5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5k OCA], [https://pdbe.org/2c5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c5k RCSB], [https://www.ebi.ac.uk/pdbsum/2c5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5k ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VPS51_YEAST VPS51_YEAST]] Involved in retrograde transport from early and late endosomes to late Golgi. Links the Golgi-associated retrograde protein (GARP) complex to the t-SNARE TLG1, leading to the fusion between the endosomal vesicles with the late Golgi. May also be indirectly involved in apical bud growth.<ref>PMID:11957109</ref> <ref>PMID:12377769</ref> <ref>PMID:12134085</ref> <ref>PMID:12446664</ref> <ref>PMID:12686613</ref>  [[http://www.uniprot.org/uniprot/TLG1_YEAST TLG1_YEAST]] SNARE protein (of Qc type) involved in membrane fusion probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. Upon vesicle tethering to the target membrane, which requires additional proteins, a SNARE-pin is formed. This is a very stable 4 parallel alpha-helical coil bundle consisting of 4 SNARE domains (usually one of each type: Qa, Qb, Qc, and R), of which at least one is anchored in the opposite membrane. The formation of the SNARE-pin is believed to bring the two membranes in close proximity and to provide the energy to drive membrane fusion. Through its interaction with the VFT (or GARP) complex, it may also contribute to vesicle recognition specificity and tethering. Regulation of SNARE-pin formation also seems to depend on the phosphorylation state of the protein, phosphorylation by TPK1 causing inhibition and dephosphorylation by SIT4 activation.<ref>PMID:9427746</ref> <ref>PMID:10397773</ref> <ref>PMID:11689439</ref> <ref>PMID:11739407</ref> <ref>PMID:12377769</ref> <ref>PMID:12686613</ref>
+[https://www.uniprot.org/uniprot/VPS51_YEAST VPS51_YEAST] Involved in retrograde transport from early and late endosomes to late Golgi. Links the Golgi-associated retrograde protein (GARP) complex to the t-SNARE TLG1, leading to the fusion between the endosomal vesicles with the late Golgi. May also be indirectly involved in apical bud growth.<ref>PMID:11957109</ref> <ref>PMID:12377769</ref> <ref>PMID:12134085</ref> <ref>PMID:12446664</ref> <ref>PMID:12686613</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Evans, P R]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Fridmann-Sirkis, Y]]
+[[Category: Evans PR]]
-[[Category: Kent, H M]]
+[[Category: Fridmann-Sirkis Y]]
-[[Category: Lewis, M J]]
+[[Category: Kent HM]]
-[[Category: Pelham, H R.B]]
+[[Category: Lewis MJ]]
-[[Category: Phosphorylation]]
+[[Category: Pelham HRB]]
-[[Category: Protein transport]]
-[[Category: Protein transport-complex]]
-[[Category: Snare]]
-[[Category: Vft complex]]