4uuy
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4uuy is ON HOLD until Paper Publication Authors: Behrmann, H., Gohlke, U., Heinemann, U. Description: Structural Identification of the Vps18 beta-p...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural Identification of the Vps18 beta-propeller reveals a critical role in the HOPS complex stability and function.== | |
| + | <StructureSection load='4uuy' size='340' side='right'caption='[[4uuy]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4uuy]] 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=4UUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UUY 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]] 2.14Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=4uuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uuy OCA], [https://pdbe.org/4uuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uuy RCSB], [https://www.ebi.ac.uk/pdbsum/4uuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uuy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PEP3_YEAST PEP3_YEAST] Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.<ref>PMID:10978279</ref> <ref>PMID:16601699</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Membrane fusion at the vacuole, the lysosome equivalent in yeast, requires the HOPS tethering complex, which is recruited by the Rab7 GTPase Ypt7. HOPS provides a template for the assembly of SNAREs and thus likely confers fusion at a distinct position on vacu-oles. Five of the six subunits in HOPS have a similar domain prediction with strong simi-larity to COPII subunits and nuclear porins. Here, we show that Vps18 indeed has a 7-bladed beta-propeller as its N-terminal domain by revealing its structure at 2.14 Angstroem. The Vps18 N-terminal domain can interact with the N-terminal part of Vps11 and also binds to lipids. Although deletion of the Vps18 N-terminal domain does not preclude HOPS assembly, as revealed by negative stain elec-tron microscopy, the complex is instable and cannot support membrane fusion in vitro. We thus conclude that the beta-propeller of Vps18 is required for HOPS stability and function, and that it can serve as a starting point for further structural analyses of the HOPS tethering complex. | ||
| - | + | Structural identification of the VPS18 beta-propeller reveals a critical role in the hops complex stability and function.,Behrmann H, Lurick A, Kuhlee A, Balderhaar HK, Brocker C, Kummel D, Engelbrecht-Vandre S, Gohlke U, Raunser S, Heinemann U, Ungermann C J Biol Chem. 2014 Oct 16. pii: jbc.M114.602714. PMID:25324549<ref>PMID:25324549</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4uuy" 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: Behrmann H]] | ||
| + | [[Category: Gohlke U]] | ||
| + | [[Category: Heinemann U]] | ||
Current revision
Structural Identification of the Vps18 beta-propeller reveals a critical role in the HOPS complex stability and function.
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