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== | ==Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of GARP to a family of tethering complexes== | ||
[[http://www.uniprot.org/uniprot/VPS53_YEAST VPS53_YEAST | <StructureSection load='3ns4' size='340' side='right'caption='[[3ns4]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ns4]] is a 1 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=3NS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NS4 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3ns4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ns4 OCA], [https://pdbe.org/3ns4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ns4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ns4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ns4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VPS53_YEAST VPS53_YEAST] Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.<ref>PMID:10637310</ref> <ref>PMID:11689439</ref> <ref>PMID:12377769</ref> <ref>PMID:12446664</ref> <ref>PMID:12686613</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ns/3ns4_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ns4 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Golgi-associated retrograde protein (GARP) complex is a membrane-tethering complex that functions in traffic from endosomes to the trans-Golgi network. Here we present the structure of a C-terminal fragment of the Vps53 subunit, important for binding endosome-derived vesicles, at a resolution of 2.9 A. We show that the C terminus consists of two alpha-helical bundles arranged in tandem, and we identify a highly conserved surface patch, which may play a role in vesicle recognition. Mutations of the surface result in defects in membrane traffic. The fold of the Vps53 C terminus is strongly reminiscent of proteins that belong to three other tethering complexes--Dsl1, conserved oligomeric Golgi, and the exocyst--thought to share a common evolutionary origin. Thus, the structure of the Vps53 C terminus suggests that GARP belongs to this family of complexes. | |||
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes.,Vasan N, Hutagalung A, Novick P, Reinisch KM Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14176-81. Epub 2010 Jul 26. PMID:20660722<ref>PMID:20660722</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
<div class="pdbe-citations 3ns4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Reinisch | [[Category: Reinisch KM]] | ||
[[Category: Vasan | [[Category: Vasan N]] | ||
Latest revision as of 11:04, 9 October 2024
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of GARP to a family of tethering complexesStructure of a C-terminal fragment of its Vps53 subunit suggests similarity of GARP to a family of tethering complexes
Structural highlights
FunctionVPS53_YEAST Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.[1] [2] [3] [4] [5] 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 PubMedThe Golgi-associated retrograde protein (GARP) complex is a membrane-tethering complex that functions in traffic from endosomes to the trans-Golgi network. Here we present the structure of a C-terminal fragment of the Vps53 subunit, important for binding endosome-derived vesicles, at a resolution of 2.9 A. We show that the C terminus consists of two alpha-helical bundles arranged in tandem, and we identify a highly conserved surface patch, which may play a role in vesicle recognition. Mutations of the surface result in defects in membrane traffic. The fold of the Vps53 C terminus is strongly reminiscent of proteins that belong to three other tethering complexes--Dsl1, conserved oligomeric Golgi, and the exocyst--thought to share a common evolutionary origin. Thus, the structure of the Vps53 C terminus suggests that GARP belongs to this family of complexes. Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes.,Vasan N, Hutagalung A, Novick P, Reinisch KM Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14176-81. Epub 2010 Jul 26. PMID:20660722[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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