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== | ==N-terminal domain of tlg1 complexed with N-terminus of vps51== | ||
Membrane fusion in cells involves the interaction of SNARE proteins on | <StructureSection load='2c5k' size='340' side='right'caption='[[2c5k]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</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'>[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 == | |||
[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 == | |||
Membrane fusion in cells involves the interaction of SNARE proteins on apposing membranes. Formation of SNARE complexes is preceded by tethering events, and a number of protein complexes that are thought to mediate this have been identified. The VFT or GARP complex is required for endosome-Golgi traffic in yeast. It consists of four subunits, one of which, Vps51, has been shown to bind specifically to the SNARE Tlg1, which participates in the same fusion event. We have determined the structure of the N-terminal domain of Tlg1 bound to a peptide from the N terminus of Vps51. Binding depends mainly on residues 18-30 of Vps51. These form a short helix which lies in a conserved groove in the three-helix bundle formed by Tlg1. Surprisingly, although both Vps51 and Tlg1 are required for transport to the late Golgi from endosomes, removal of the Tlg1-binding sequences from Vps51 does not block such traffic in vivo. Thus, this particular interaction cannot be crucial to the process of vesicle docking or fusion. | |||
Structural analysis of the interaction between the SNARE Tlg1 and Vps51.,Fridmann-Sirkis Y, Kent HM, Lewis MJ, Evans PR, Pelham HR Traffic. 2006 Feb;7(2):182-90. PMID:16420526<ref>PMID:16420526</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2c5k" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Evans | [[Category: Evans PR]] | ||
[[Category: Fridmann-Sirkis | [[Category: Fridmann-Sirkis Y]] | ||
[[Category: Kent | [[Category: Kent HM]] | ||
[[Category: Lewis | [[Category: Lewis MJ]] | ||
[[Category: Pelham | [[Category: Pelham HRB]] | ||
Latest revision as of 13:24, 6 September 2023
N-terminal domain of tlg1 complexed with N-terminus of vps51N-terminal domain of tlg1 complexed with N-terminus of vps51
Structural highlights
FunctionVPS51_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.[1] [2] [3] [4] [5] Publication Abstract from PubMedMembrane fusion in cells involves the interaction of SNARE proteins on apposing membranes. Formation of SNARE complexes is preceded by tethering events, and a number of protein complexes that are thought to mediate this have been identified. The VFT or GARP complex is required for endosome-Golgi traffic in yeast. It consists of four subunits, one of which, Vps51, has been shown to bind specifically to the SNARE Tlg1, which participates in the same fusion event. We have determined the structure of the N-terminal domain of Tlg1 bound to a peptide from the N terminus of Vps51. Binding depends mainly on residues 18-30 of Vps51. These form a short helix which lies in a conserved groove in the three-helix bundle formed by Tlg1. Surprisingly, although both Vps51 and Tlg1 are required for transport to the late Golgi from endosomes, removal of the Tlg1-binding sequences from Vps51 does not block such traffic in vivo. Thus, this particular interaction cannot be crucial to the process of vesicle docking or fusion. Structural analysis of the interaction between the SNARE Tlg1 and Vps51.,Fridmann-Sirkis Y, Kent HM, Lewis MJ, Evans PR, Pelham HR Traffic. 2006 Feb;7(2):182-90. PMID:16420526[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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