4uuy: Difference between revisions
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''' | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UUY FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uuy RCSB], [http://www.ebi.ac.uk/pdbsum/4uuy PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Behrmann, H.]] | |||
[[Category: Gohlke, U.]] | |||
[[Category: Heinemann, U.]] | |||
[[Category: Endosome]] | |||
[[Category: Hop]] | |||
[[Category: Membrane fusion]] | |||
[[Category: Transport protein]] | |||
[[Category: Vacuole]] | |||
Revision as of 11:10, 29 October 2014
Structural Identification of the Vps18 beta-propeller reveals a critical role in the HOPS complex stability and function.
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